ITPKA: Difference between revisions

Jump to navigation Jump to search
← Older edit
VisualWikitext
Matt Pijoan (talk | contribs)
Bots, Bureaucrats, bureaucrats, Interface administrators, interwiki, nocaptcha, smwadministrator, staff, Administrators, Widget editors
7,579 edits
m 1 revision imported
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
{{Underlinked|date=March 2014}}
{{Infobox_gene}}
{{Infobox_gene}}
'''Inositol-trisphosphate 3-kinase A''' is an [[enzyme]] that in humans is encoded by the ''ITPKA'' [[gene]].<ref name="pmid1330886">{{cite journal |vauthors=Erneux C, Roeckel N, Takazawa K, Mailleux P, Vassart G, Mattei MG | title = Localization of the genes for human inositol 1,4,5-trisphosphate 3-kinase A (ITPKA) and B (ITPKB) to chromosome regions 15q14-q21 and 1q41-q43, respectively, by in situ hybridization | journal = Genomics | volume = 14 | issue = 2 | pages = 546–7 |date=Dec 1992 | pmid = 1330886 | pmc =  | doi =10.1016/S0888-7543(05)80265-4  }}</ref><ref name="pmid2175886">{{cite journal |vauthors=Takazawa K, Perret J, Dumont JE, Erneux C | title = Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence | journal = Nucleic Acids Res | volume = 18 | issue = 23 | pages = 7141 |date=Feb 1991 | pmid = 2175886 | pmc = 332787 | doi =10.1093/nar/18.23.7141  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3706| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
'''Inositol-trisphosphate 3-kinase A''' is an [[enzyme]] that in humans is encoded by the ''ITPKA'' [[gene]].<ref name="pmid1330886">{{cite journal | vauthors = Erneux C, Roeckel N, Takazawa K, Mailleux P, Vassart G, Mattei MG | title = Localization of the genes for human inositol 1,4,5-trisphosphate 3-kinase A (ITPKA) and B (ITPKB) to chromosome regions 15q14-q21 and 1q41-q43, respectively, by in situ hybridization | journal = Genomics | volume = 14 | issue = 2 | pages = 546–7 | date = October 1992 | pmid = 1330886 | pmc = | doi = 10.1016/S0888-7543(05)80265-4 }}</ref><ref name="pmid2175886">{{cite journal | vauthors = Takazawa K, Perret J, Dumont JE, Erneux C | title = Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence | journal = Nucleic Acids Research | volume = 18 | issue = 23 | pages = 7141 | date = December 1990 | pmid = 2175886 | pmc = 332787 | doi = 10.1093/nar/18.23.7141 }}</ref><ref>name="entrez"{{cite web | title = Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3706 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text = Regulates inositol phosphate metabolism by phosphorylation of second messenger inositol 1,4,5-trisphosphate to Ins(1,3,4,5)P4. The activity of the inositol 1,4,5-trisphosphate 3-kinase is responsible for regulating the levels of a large number of inositol polyphosphates that are important in cellular signaling. Both calcium/calmodulin and protein phosphorylation mechanisms control its activity. It is also a substrate for the cyclic AMP-dependent protein kinase, calcium/calmodulin- dependent protein kinase II, and protein kinase C in vitro. ITPKA and ITPKB are 68% identical in the C-terminus region.<ref name="entrez" />
}}


==References==
== Structure ==
{{reflist}}
ITPKA is one of three inositol-trisphosphate 3-kinase (ITP3K) genes in humans. [[Inositol-trisphosphate 3-kinase|ITP3K]] proteins regulate [[inositol phosphate]] metabolism by [[phosphorylation]] of the second messenger [[inositol 1,4,5-trisphosphate]] to produce Ins(1,3,4,5)P<small>4</small>, which is sometimes abbreviated as IP<small>4</small>. Structurally, ITPKA belongs to the [[inositol polyphosphate kinase]] (IPK) family. The activity of the inositol 1,4,5-trisphosphate 3-kinase is responsible for regulating the levels of a large number of inositol polyphosphates that are important in cellular signaling, most notably, [[inositol trisphosphate]], which is the enzyme's only substrate. Both calcium/[[calmodulin]] and protein phosphorylation mechanisms control its activity. It is also a substrate for the [[Protein kinase A|cyclic AMP-dependent protein kinase]], [[Ca2+/calmodulin-dependent protein kinase II|calcium/calmodulin- dependent protein kinase II]], and [[protein kinase C]] in vitro. ITPKA and ITPKB are 68% identical in the [[C-terminus]] region The amino- terminal region of ITPKA binds filamentous [[actin]]. This property localizes the ITPKA to [[dendritic spine]]s in principal neurons.<ref name="pmid8387863">{{cite journal | vauthors = Yamada M, Kakita A, Mizuguchi M, Rhee SG, Kim SU, Ikuta F | title = Specific expression of inositol 1,4,5-trisphosphate 3-kinase in dendritic spines | journal = Brain Research | volume = 606 | issue = 2 | pages = 335–40 | date = March 1993 | pmid = 8387863 | pmc = | doi = }}</ref><ref name="pmid11468283">{{cite journal | vauthors = Schell MJ, Erneux C, Irvine RF | title = Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus | journal = The Journal of Biological Chemistry | volume = 276 | issue = 40 | pages = 37537–46 | date = October 2001 | pmid = 11468283 | pmc = | doi = 10.1074/jbc.M104101200 }}</ref><ref name="pmid22120525">{{cite journal | vauthors = Windhorst S, Minge D, Bähring R, Hüser S, Schob C, Blechner C, Lin HY, Mayr GW, Kindler S | title = Inositol-1,4,5-trisphosphate 3-kinase A regulates dendritic morphology and shapes synaptic Ca2+ transients | journal = Cellular Signalling | volume = 24 | issue = 3 | pages = 750–7 | date = March 2012 | pmid = 22120525 | pmc = | doi = 10.1016/j.cellsig.2011.11.010 }}</ref> ITPKA is expressed physiologically in neurons, but it is sometimes expressed in cancer cells and may contribute to processes of metastasis.<ref name="pmid20022963">{{cite journal | vauthors = Windhorst S, Fliegert R, Blechner C, Möllmann K, Hosseini Z, Günther T, Eiben M, Chang L, Lin HY, Fanick W, Schumacher U, Brandt B, Mayr GW | title = Inositol 1,4,5-trisphosphate 3-kinase-A is a new cell motility-promoting protein that increases the metastatic potential of tumor cells by two functional activities | journal = The Journal of Biological Chemistry | volume = 285 | issue = 8 | pages = 5541–54 | date = February 2010 | pmid = 20022963 | pmc = 2820782 | doi = 10.1074/jbc.M109.047050 }}</ref>


==Further reading==
== Physiological function ==
ITPKA participates in learning and memory processes in neurons.<ref name="pmid27053114">{{cite journal | vauthors = Chung S, Kim IH, Lee D, Park K, Kim JY, Lee YK, Kim EJ, Lee HW, Choi JS, Son GH, Sun W, Shin KS, Kim H | title = The role of inositol 1,4,5-trisphosphate 3-kinase A in regulating emotional behavior and amygdala function | journal = Scientific Reports | volume = 6 | issue = | pages = 23757 | date = April 2016 | pmid = 27053114 | pmc = 4823716 | doi = 10.1038/srep23757 }}</ref><ref name="pmid29617377">{{cite journal | vauthors = Choi B, Lee HW, Mo S, Kim JY, Kim HW, Rhyu IJ, Hong E, Lee YK, Choi JS, Kim CH, Kim H | title = Inositol 1,4,5-trisphosphate 3-kinase A overexpressed in mouse forebrain modulates synaptic transmission and mGluR-LTD of CA1 pyramidal neurons | journal = PLOS One | volume = 13 | issue = 4 | pages = e0193859 | year = 2018 | pmid = 29617377 | pmc = 5884490 | doi = 10.1371/journal.pone.0193859 }}</ref>
 
== Roles in human disease ==
Although ITPKA is expressed physiologically in neurons and testis, it sometimes becomes expressed in cancer cells, and the expression usually makes the cancer more aggressive.<ref name="pmid20022963"/><ref name="pmid28377279">{{cite journal | vauthors = Windhorst S, Song K, Gazdar AF | title = Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types | journal = Biochemical Pharmacology | volume = 137 | issue = | pages = 1–9 | date = August 2017 | pmid = 28377279 | pmc = 5555585 | doi = 10.1016/j.bcp.2017.03.023 }}</ref>
 
== Relationship to F-tractin ==
[[F-tractin]] is amino acids 9-52 of rat ITPKA. It was later determined that amino acids 9-40 were sufficient for binding filamentous actin.<ref name="pmid19846664">{{cite journal | vauthors = Johnson HW, Schell MJ | title = Neuronal IP3 3-kinase is an F-actin-bundling protein: role in dendritic targeting and regulation of spine morphology | journal = Molecular Biology of the Cell | volume = 20 | issue = 24 | pages = 5166–80 | date = December 2009 | pmid = 19846664 | pmc = 2793293 | doi = 10.1091/mbc.E09-01-0083 }}</ref><ref name="pmid22219382">{{cite journal | vauthors = Yi J, Wu XS, Crites T, Hammer JA | title = Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells | journal = Molecular Biology of the Cell | volume = 23 | issue = 5 | pages = 834–52 | date = March 2012 | pmid = 22219382 | pmc = 3290643 | doi = 10.1091/mbc.E11-08-0731 }}</ref> When fused to a reporter, such as [[green fluorescent protein]], It is useful for the vsualization of actin dynamics in living cells.<ref name="pmid26317264">{{cite journal | vauthors = Belin BJ, Goins LM, Mullins RD | title = Comparative analysis of tools for live cell imaging of actin network architecture | journal = Bioarchitecture | volume = 4 | issue = 6 | pages = 189–202 | year = 2014 | pmid = 26317264 | pmc = 4914014 | doi = 10.1080/19490992.2014.1047714 }}</ref><ref name="pmid28082420">{{cite journal | vauthors = Melak M, Plessner M, Grosse R | title = Actin visualization at a glance | journal = Journal of Cell Science | volume = 130 | issue = 3 | pages = 525–530 | date = February 2017 | pmid = 28082420 | pmc = | doi = 10.1242/jcs.189068 }}</ref>
 
== References ==
{{Reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Takazawa K, Perret J, Dumont JE, Erneux C | title = Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme | journal = The Biochemical Journal | volume = 278 ( Pt 3) | issue = Pt 3 | pages = 883–6 | date = September 1991 | pmid = 1654894 | pmc = 1151429 | doi = }}
| citations =
* {{cite journal | vauthors = Takazawa K, Erneux C | title = Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase | journal = The Biochemical Journal | volume = 280 ( Pt 1) | issue = Pt 1 | pages = 125–9 | date = November 1991 | pmid = 1660262 | pmc = 1130609 | doi = }}
*{{cite journal |vauthors=Takazawa K, Perret J, Dumont JE, Erneux C |title=Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme |journal=Biochem. J. |volume=278 ( Pt 3) |issue= Pt 3|pages= 883–6 |year= 1991 |pmid= 1654894 |doi= | pmc=1151429  }}
* {{cite journal | vauthors = Takazawa K, Perret J, Dumont JE, Erneux C | title = Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase | journal = Biochemical and Biophysical Research Communications | volume = 174 | issue = 2 | pages = 529–35 | date = January 1991 | pmid = 1847047 | doi = 10.1016/0006-291X(91)91449-M }}
*{{cite journal |vauthors=Takazawa K, Erneux C |title=Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase |journal=Biochem. J. |volume=280 ( Pt 1) |issue= Pt 1|pages= 125–9 |year= 1992 |pmid= 1660262 |doi= | pmc=1130609  }}
* {{cite journal | vauthors = Lin AN, Barnes S, Wallace RW | title = Phosphorylation by protein kinase C inactivates an inositol 1,4,5-trisphosphate 3-kinase purified from human platelets | journal = Biochemical and Biophysical Research Communications | volume = 170 | issue = 3 | pages = 1371–6 | date = August 1990 | pmid = 2167676 | doi = 10.1016/0006-291X(90)90546-Y }}
*{{cite journal |vauthors=Takazawa K, Perret J, Dumont JE, Erneux C |title=Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase |journal=Biochem. Biophys. Res. Commun. |volume=174 |issue= 2 |pages= 529–35 |year= 1991 |pmid= 1847047 |doi=10.1016/0006-291X(91)91449-M }}
* {{cite journal | vauthors = Takazawa K, Vandekerckhove J, Dumont JE, Erneux C | title = Cloning and expression in Escherichia coli of a rat brain cDNA encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase | journal = The Biochemical Journal | volume = 272 | issue = 1 | pages = 107–12 | date = November 1990 | pmid = 2176078 | pmc = 1149663 | doi = }}
*{{cite journal |vauthors=Lin AN, Barnes S, Wallace RW |title=Phosphorylation by protein kinase C inactivates an inositol 1,4,5-trisphosphate 3-kinase purified from human platelets |journal=Biochem. Biophys. Res. Commun. |volume=170 |issue= 3 |pages= 1371–6 |year= 1990 |pmid= 2167676 |doi=10.1016/0006-291X(90)90546-Y }}
* {{cite journal | vauthors = Ryu SH, Lee SY, Lee KY, Rhee SG | title = Catalytic properties of inositol trisphosphate kinase: activation by Ca2+ and calmodulin | journal = FASEB Journal | volume = 1 | issue = 5 | pages = 388–93 | date = November 1987 | pmid = 2824270 | doi = }}
*{{cite journal |vauthors=Takazawa K, Vandekerckhove J, Dumont JE, Erneux C |title=Cloning and expression in Escherichia coli of a rat brain cDNA encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase |journal=Biochem. J. |volume=272 |issue= 1 |pages= 107–12 |year= 1991 |pmid= 2176078 |doi= | pmc=1149663  }}
* {{cite journal | vauthors = Communi D, Vanweyenberg V, Erneux C | title = D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism | journal = The EMBO Journal | volume = 16 | issue = 8 | pages = 1943–52 | date = April 1997 | pmid = 9155020 | pmc = 1169797 | doi = 10.1093/emboj/16.8.1943 }}
*{{cite journal |vauthors=Ryu SH, Lee SY, Lee KY, Rhee SG |title=Catalytic properties of inositol trisphosphate kinase: activation by Ca2+ and calmodulin |journal=FASEB J. |volume=1 |issue= 5 |pages= 388–93 |year= 1987 |pmid= 2824270 |doi= }}
* {{cite journal | vauthors = Woodring PJ, Garrison JC | title = Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase | journal = The Journal of Biological Chemistry | volume = 272 | issue = 48 | pages = 30447–54 | date = November 1997 | pmid = 9374536 | doi = 10.1074/jbc.272.48.30447 }}
*{{cite journal |vauthors=Communi D, Vanweyenberg V, Erneux C |title=D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism |journal=EMBO J. |volume=16 |issue= 8 |pages= 1943–52 |year= 1997 |pmid= 9155020 |doi= 10.1093/emboj/16.8.1943 | pmc=1169797 }}
* {{cite journal | vauthors = Schell MJ, Erneux C, Irvine RF | title = Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus | journal = The Journal of Biological Chemistry | volume = 276 | issue = 40 | pages = 37537–46 | date = October 2001 | pmid = 11468283 | doi = 10.1074/jbc.M104101200 }}
*{{cite journal |vauthors=Woodring PJ, Garrison JC |title=Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30447–54 |year= 1997 |pmid= 9374536 |doi=10.1074/jbc.272.48.30447 }}
* {{cite journal | vauthors = Mishra J, Bhalla US | title = Simulations of inositol phosphate metabolism and its interaction with InsP(3)-mediated calcium release | journal = Biophysical Journal | volume = 83 | issue = 3 | pages = 1298–316 | date = September 2002 | pmid = 12202356 | pmc = 1302229 | doi = 10.1016/S0006-3495(02)73901-5 }}
*{{cite journal |vauthors=Schell MJ, Erneux C, Irvine RF |title=Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37537–46 |year= 2001 |pmid= 11468283 |doi= 10.1074/jbc.M104101200 }}
* {{cite journal | vauthors = Dewaste V, Moreau C, De Smedt F, Bex F, De Smedt H, Wuytack F, Missiaen L, Erneux C | title = The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells | journal = The Biochemical Journal | volume = 374 | issue = Pt 1 | pages = 41–9 | date = August 2003 | pmid = 12747803 | pmc = 1223573 | doi = 10.1042/BJ20021963 }}
*{{cite journal |vauthors=Mishra J, Bhalla US |title=Simulations of inositol phosphate metabolism and its interaction with InsP(3)-mediated calcium release |journal=Biophys. J. |volume=83 |issue= 3 |pages= 1298–316 |year= 2003 |pmid= 12202356 |doi=10.1016/S0006-3495(02)73901-5 | pmc=1302229  }}
* {{cite journal | vauthors = González B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL | title = Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase | journal = Molecular Cell | volume = 15 | issue = 5 | pages = 689–701 | date = September 2004 | pmid = 15350214 | doi = 10.1016/j.molcel.2004.08.004 }}
*{{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
* {{cite journal | vauthors = Kato H, Uzawa K, Onda T, Kato Y, Saito K, Nakashima D, Ogawara K, Bukawa H, Yokoe H, Tanzawa H | title = Down-regulation of 1D-myo-inositol 1,4,5-trisphosphate 3-kinase A protein expression in oral squamous cell carcinoma | journal = International Journal of Oncology | volume = 28 | issue = 4 | pages = 873–81 | date = April 2006 | pmid = 16525636 | doi = 10.3892/ijo.28.4.873 }}
*{{cite journal  | author=Dewaste V |title=The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells |journal=Biochem. J. |volume=374 |issue= Pt 1 |pages= 41–9 |year= 2003 |pmid= 12747803 |doi= 10.1042/BJ20021963 | pmc=1223573  |name-list-format=vanc| author2=Moreau C  | author3=De Smedt F  | display-authors=3  | last4=Bex  | first4=Françoise  | last5=De Smedt  | first5=Humbert  | last6=Wuytack  | first6=Frank  | last7=Missiaen  | first7=Ludwig  | last8=Erneux  | first8=Christophe }}
*{{cite journal | author=González B |title=Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase |journal=Mol. Cell |volume=15 |issue= 5 |pages= 689–701 |year= 2004 |pmid= 15350214 |doi= 10.1016/j.molcel.2004.08.004 |name-list-format=vanc| author2=Schell MJ  | author3=Letcher AJ  | display-authors=3  | last4=Veprintsev  | first4=Dmitry B.  | last5=Irvine  | first5=Robin F.  | last6=Williams  | first6=Roger L. }}
*{{cite journal | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Kato H |title=Down-regulation of 1D-myo-inositol 1,4,5-trisphosphate 3-kinase A protein expression in oral squamous cell carcinoma |journal=Int. J. Oncol. |volume=28 |issue= 4 |pages= 873–81 |year= 2006 |pmid= 16525636 |doi= 10.3892/ijo.28.4.873|name-list-format=vanc| author2=Uzawa K  | author3=Onda T  | display-authors=3  | last4=Kato  | first4=Y  | last5=Saito  | first5=K  | last6=Nakashima  | first6=D  | last7=Ogawara  | first7=K  | last8=Bukawa  | first8=H  | last9=Yokoe  | first9=H  }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3706}}
{{PDB Gallery|geneid=3706}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
{{gene-15-stub}}

Latest revision as of 12:44, 9 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Inositol-trisphosphate 3-kinase A is an enzyme that in humans is encoded by the ITPKA gene.[1][2][3]

Structure

ITPKA is one of three inositol-trisphosphate 3-kinase (ITP3K) genes in humans. ITP3K proteins regulate inositol phosphate metabolism by phosphorylation of the second messenger inositol 1,4,5-trisphosphate to produce Ins(1,3,4,5)P4, which is sometimes abbreviated as IP4. Structurally, ITPKA belongs to the inositol polyphosphate kinase (IPK) family. The activity of the inositol 1,4,5-trisphosphate 3-kinase is responsible for regulating the levels of a large number of inositol polyphosphates that are important in cellular signaling, most notably, inositol trisphosphate, which is the enzyme's only substrate. Both calcium/calmodulin and protein phosphorylation mechanisms control its activity. It is also a substrate for the cyclic AMP-dependent protein kinase, calcium/calmodulin- dependent protein kinase II, and protein kinase C in vitro. ITPKA and ITPKB are 68% identical in the C-terminus region The amino- terminal region of ITPKA binds filamentous actin. This property localizes the ITPKA to dendritic spines in principal neurons.[4][5][6] ITPKA is expressed physiologically in neurons, but it is sometimes expressed in cancer cells and may contribute to processes of metastasis.[7]

Physiological function

ITPKA participates in learning and memory processes in neurons.[8][9]

Roles in human disease

Although ITPKA is expressed physiologically in neurons and testis, it sometimes becomes expressed in cancer cells, and the expression usually makes the cancer more aggressive.[7][10]

Relationship to F-tractin

F-tractin is amino acids 9-52 of rat ITPKA. It was later determined that amino acids 9-40 were sufficient for binding filamentous actin.[11][12] When fused to a reporter, such as green fluorescent protein, It is useful for the vsualization of actin dynamics in living cells.[13][14]

References

  1. ↑ Erneux C, Roeckel N, Takazawa K, Mailleux P, Vassart G, Mattei MG (October 1992). "Localization of the genes for human inositol 1,4,5-trisphosphate 3-kinase A (ITPKA) and B (ITPKB) to chromosome regions 15q14-q21 and 1q41-q43, respectively, by in situ hybridization". Genomics. 14 (2): 546–7. doi:10.1016/S0888-7543(05)80265-4. PMID 1330886.
  2. ↑ Takazawa K, Perret J, Dumont JE, Erneux C (December 1990). "Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence". Nucleic Acids Research. 18 (23): 7141. doi:10.1093/nar/18.23.7141. PMC 332787. PMID 2175886.
  3. ↑ name="entrez""Entrez Gene: ITPKA inositol 1,4,5-trisphosphate 3-kinase A".
  4. ↑ Yamada M, Kakita A, Mizuguchi M, Rhee SG, Kim SU, Ikuta F (March 1993). "Specific expression of inositol 1,4,5-trisphosphate 3-kinase in dendritic spines". Brain Research. 606 (2): 335–40. PMID 8387863.
  5. ↑ Schell MJ, Erneux C, Irvine RF (October 2001). "Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus". The Journal of Biological Chemistry. 276 (40): 37537–46. doi:10.1074/jbc.M104101200. PMID 11468283.
  6. ↑ Windhorst S, Minge D, Bähring R, Hüser S, Schob C, Blechner C, Lin HY, Mayr GW, Kindler S (March 2012). "Inositol-1,4,5-trisphosphate 3-kinase A regulates dendritic morphology and shapes synaptic Ca2+ transients". Cellular Signalling. 24 (3): 750–7. doi:10.1016/j.cellsig.2011.11.010. PMID 22120525.
  7. ↑ 7.0 7.1 Windhorst S, Fliegert R, Blechner C, Möllmann K, Hosseini Z, Günther T, Eiben M, Chang L, Lin HY, Fanick W, Schumacher U, Brandt B, Mayr GW (February 2010). "Inositol 1,4,5-trisphosphate 3-kinase-A is a new cell motility-promoting protein that increases the metastatic potential of tumor cells by two functional activities". The Journal of Biological Chemistry. 285 (8): 5541–54. doi:10.1074/jbc.M109.047050. PMC 2820782. PMID 20022963.
  8. ↑ Chung S, Kim IH, Lee D, Park K, Kim JY, Lee YK, Kim EJ, Lee HW, Choi JS, Son GH, Sun W, Shin KS, Kim H (April 2016). "The role of inositol 1,4,5-trisphosphate 3-kinase A in regulating emotional behavior and amygdala function". Scientific Reports. 6: 23757. doi:10.1038/srep23757. PMC 4823716. PMID 27053114.
  9. ↑ Choi B, Lee HW, Mo S, Kim JY, Kim HW, Rhyu IJ, Hong E, Lee YK, Choi JS, Kim CH, Kim H (2018). "Inositol 1,4,5-trisphosphate 3-kinase A overexpressed in mouse forebrain modulates synaptic transmission and mGluR-LTD of CA1 pyramidal neurons". PLOS One. 13 (4): e0193859. doi:10.1371/journal.pone.0193859. PMC 5884490. PMID 29617377.
  10. ↑ Windhorst S, Song K, Gazdar AF (August 2017). "Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types". Biochemical Pharmacology. 137: 1–9. doi:10.1016/j.bcp.2017.03.023. PMC 5555585. PMID 28377279.
  11. ↑ Johnson HW, Schell MJ (December 2009). "Neuronal IP3 3-kinase is an F-actin-bundling protein: role in dendritic targeting and regulation of spine morphology". Molecular Biology of the Cell. 20 (24): 5166–80. doi:10.1091/mbc.E09-01-0083. PMC 2793293. PMID 19846664.
  12. ↑ Yi J, Wu XS, Crites T, Hammer JA (March 2012). "Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells". Molecular Biology of the Cell. 23 (5): 834–52. doi:10.1091/mbc.E11-08-0731. PMC 3290643. PMID 22219382.
  13. ↑ Belin BJ, Goins LM, Mullins RD (2014). "Comparative analysis of tools for live cell imaging of actin network architecture". Bioarchitecture. 4 (6): 189–202. doi:10.1080/19490992.2014.1047714. PMC 4914014. PMID 26317264.
  14. ↑ Melak M, Plessner M, Grosse R (February 2017). "Actin visualization at a glance". Journal of Cell Science. 130 (3): 525–530. doi:10.1242/jcs.189068. PMID 28082420.

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=ITPKA&oldid=1519525"