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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Zyxin''' is a [[protein]] that in humans is encoded by the ''ZYX'' [[gene]].<ref name="pmid8917469">{{cite journal | vauthors = Zumbrunn J, Trueb B | title = A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts | journal = Eur J Biochem | volume = 241 | issue = 2 | pages = 657–63 | date = January 1997 | pmid = 8917469 | pmc =  | doi = 10.1111/j.1432-1033.1996.00657.x }}</ref><ref name="pmid8940160">{{cite journal | vauthors = Macalma T, Otte J, Hensler ME, Bockholt SM, Louis HA, Kalff-Suske M, Grzeschik KH, von der Ahe D, Beckerle MC | title = Molecular characterization of human zyxin | journal = J Biol Chem | volume = 271 | issue = 49 | pages = 31470–8 | date = January 1997 | pmid = 8940160 | pmc = | doi = 10.1074/jbc.271.49.31470 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ZYX zyxin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7791| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Zyxin
| HGNCid = 13200
| Symbol = ZYX
| AltSymbols =; ESP-2; HED-2
| OMIM = 602002
| ECnumber = 
| Homologene = 31164
| MGIid = 103072
| GeneAtlas_image1 = PBB_GE_ZYX_200808_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ZYX_215706_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0005913 |text = cell-cell adherens junction}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7791
    | Hs_Ensembl = ENSG00000159840
    | Hs_RefseqProtein = NP_001010972
    | Hs_RefseqmRNA = NM_001010972
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 142788482
    | Hs_GenLoc_end = 142798322
    | Hs_Uniprot = Q15942
    | Mm_EntrezGene = 22793
    | Mm_Ensembl = ENSMUSG00000029860
    | Mm_RefseqmRNA = NM_011777
    | Mm_RefseqProtein = NP_035907
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 42279476
    | Mm_GenLoc_end = 42289753
    | Mm_Uniprot = Q62523
  }}
}}
'''Zyxin''', also known as '''ZYX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ZYX zyxin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7791| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Focal adhesion]]s are actin-rich structures that enable cells to adhere to the [[extracellular matrix]] and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three [[LIM domain]]s in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform.<ref name="entrez">{{cite web | title = Entrez Gene: ZYX zyxin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7791| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Reinhard M, Jouvenal K, Tripier D, Walter U |title=Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7956-60 |year= 1995 |pmid= 7644520 |doi=  }}
*{{cite journal  | author=Wang LF, Miao SY, Zong SD, ''et al.'' |title=Gene encoding a mammalian epididymal protein. |journal=Biochem. Mol. Biol. Int. |volume=34 |issue= 6 |pages= 1131-6 |year= 1995 |pmid= 7696985 |doi=  }}
*{{cite journal  | author=Hobert O, Schilling JW, Beckerle MC, ''et al.'' |title=SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin. |journal=Oncogene |volume=12 |issue= 7 |pages= 1577-81 |year= 1996 |pmid= 8622875 |doi=  }}
*{{cite journal  | author=Zumbrunn J, Trueb B |title=A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts. |journal=Eur. J. Biochem. |volume=241 |issue= 2 |pages= 657-63 |year= 1997 |pmid= 8917469 |doi=  }}
*{{cite journal  | author=Macalma T, Otte J, Hensler ME, ''et al.'' |title=Molecular characterization of human zyxin. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31470-8 |year= 1997 |pmid= 8940160 |doi=  }}
*{{cite journal  | author=Kotake K, Ozaki N, Mizuta M, ''et al.'' |title=Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells. |journal=J. Biol. Chem. |volume=272 |issue= 47 |pages= 29407-10 |year= 1997 |pmid= 9367993 |doi=  }}
*{{cite journal  | author=Zumbrunn J, Trueb B |title=Assignment of the ZYX gene for the LIM protein zyxin to human chromosome bands 7q34-->q35 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 283-4 |year= 1998 |pmid= 9730620 |doi=  }}
*{{cite journal  | author=Yang JX, Miao SY, Wu YW, ''et al.'' |title=Gene encoding a human testis Sertoli cell component related to LIM domain protein. |journal=Biochem. Mol. Biol. Int. |volume=46 |issue= 1 |pages= 11-9 |year= 1998 |pmid= 9784834 |doi=  }}
*{{cite journal  | author=Reinhard M, Zumbrunn J, Jaquemar D, ''et al.'' |title=An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13410-8 |year= 1999 |pmid= 10224105 |doi=  }}
*{{cite journal  | author=Drees B, Friederich E, Fradelizi J, ''et al.'' |title=Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22503-11 |year= 2000 |pmid= 10801818 |doi= 10.1074/jbc.M001698200 }}
*{{cite journal  | author=Hirota T, Morisaki T, Nishiyama Y, ''et al.'' |title=Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor. |journal=J. Cell Biol. |volume=149 |issue= 5 |pages= 1073-86 |year= 2000 |pmid= 10831611 |doi=  }}
*{{cite journal  | author=Smolenski A, Poller W, Walter U, Lohmann SM |title=Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25723-32 |year= 2000 |pmid= 10851246 |doi= 10.1074/jbc.M909632199 }}
*{{cite journal  | author=Harbeck B, Hüttelmaier S, Schluter K, ''et al.'' |title=Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 30817-25 |year= 2000 |pmid= 10882740 |doi= 10.1074/jbc.M005066200 }}
*{{cite journal  | author=Schenker T, Trueb B |title=BSPRY, a novel protein of the Ro-Ret family. |journal=Biochim. Biophys. Acta |volume=1493 |issue= 1-2 |pages= 255-8 |year= 2000 |pmid= 10978534 |doi=  }}
*{{cite journal  | author=Li B, Trueb B |title=Analysis of the alpha-actinin/zyxin interaction. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 33328-35 |year= 2001 |pmid= 11423549 |doi= 10.1074/jbc.M100789200 }}
*{{cite journal  | author=Degenhardt YY, Silverstein S |title=Interaction of zyxin, a focal adhesion protein, with the e6 protein from human papillomavirus type 6 results in its nuclear translocation. |journal=J. Virol. |volume=75 |issue= 23 |pages= 11791-802 |year= 2001 |pmid= 11689660 |doi= 10.1128/JVI.75.23.11791-11802.2001 }}
*{{cite journal  | author=Yi J, Kloeker S, Jensen CC, ''et al.'' |title=Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9580-9 |year= 2002 |pmid= 11782456 |doi= 10.1074/jbc.M106922200 }}
*{{cite journal  | author=van der Gaag EJ, Leccia MT, Dekker SK, ''et al.'' |title=Role of zyxin in differential cell spreading and proliferation of melanoma cells and melanocytes. |journal=J. Invest. Dermatol. |volume=118 |issue= 2 |pages= 246-54 |year= 2002 |pmid= 11841540 |doi= 10.1046/j.0022-202x.2001.01657.x }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal  | author=Scherer SW, Cheung J, MacDonald JR, ''et al.'' |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767-72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423 }}
}}
{{refend}}


{{protein-stub}}
Zyxin has been shown to [[Protein-protein interaction|interact]] with:
{{WikiDoc Sources}}
* [[Actinin, alpha 1]]<ref name = pmid10224105>{{cite journal | vauthors = Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B | title = An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment | journal = J. Biol. Chem. | volume = 274 | issue = 19 | pages = 13410–8 | date = May 1999 | pmid = 10224105 | doi =  10.1074/jbc.274.19.13410}}</ref><ref name = pmid11423549>{{cite journal | vauthors = Li B, Trueb B | title = Analysis of the alpha-actinin/zyxin interaction | journal = J. Biol. Chem. | volume = 276 | issue = 36 | pages = 33328–35 | date = September 2001 | pmid = 11423549 | doi = 10.1074/jbc.M100789200 }}</ref>
* [[ENAH (gene)|ENAH]],<ref name = pmid12672821>{{cite journal | vauthors = Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H, Shishido T | title = Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase | journal = J. Biol. Chem. | volume = 278 | issue = 24 | pages = 21685–92 | date = June 2003 | pmid = 12672821 | doi = 10.1074/jbc.M301447200 }}</ref><ref name = pmid10801818>{{cite journal | vauthors = Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM | title = Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins | journal = J. Biol. Chem. | volume = 275 | issue = 29 | pages = 22503–11 | date = July 2000 | pmid = 10801818 | doi = 10.1074/jbc.M001698200 }}</ref>
* [[LASP1]],<ref name = pmid15004028>{{cite journal | vauthors = Li B, Zhuang L, Trueb B | title = Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1 | journal = J. Biol. Chem. | volume = 279 | issue = 19 | pages = 20401–10 | date = May 2004 | pmid = 15004028 | doi = 10.1074/jbc.M310304200 }}</ref>
* [[LATS1]],<ref name = pmid10831611>{{cite journal | vauthors = Hirota T, Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H | title = Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor | journal = J. Cell Biol. | volume = 149 | issue = 5 | pages = 1073–86 | date = May 2000 | pmid = 10831611 | pmc = 2174824 | doi =  10.1083/jcb.149.5.1073}}</ref>  and
* [[Vasodilator-stimulated phosphoprotein]].<ref name = pmid10801818/><ref name = pmid10882740>{{cite journal | vauthors = Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S | title = Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin | journal = J. Biol. Chem. | volume = 275 | issue = 40 | pages = 30817–25 | date = October 2000 | pmid = 10882740 | doi = 10.1074/jbc.M005066200 }}</ref>
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = Reinhard M, Jouvenal K, Tripier D, Walter U | title = Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein) | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 17 | pages = 7956–60 | year = 1995 | pmid = 7644520 | pmc = 41265 | doi = 10.1073/pnas.92.17.7956 }}
* {{cite journal | vauthors = Wang LF, Miao SY, Zong SD, Bai Y, Koide SS | title = Gene encoding a mammalian epididymal protein | journal = Biochem. Mol. Biol. Int. | volume = 34 | issue = 6 | pages = 1131–6 | year = 1995 | pmid = 7696985 | doi =  }}
* {{cite journal | vauthors = Hobert O, Schilling JW, Beckerle MC, Ullrich A, Jallal B | title = SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin | journal = Oncogene | volume = 12 | issue = 7 | pages = 1577–81 | year = 1996 | pmid = 8622875 | doi =  }}
* {{cite journal | vauthors = Kotake K, Ozaki N, Mizuta M, Sekiya S, Inagaki N, Seino S | title = Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells | journal = J. Biol. Chem. | volume = 272 | issue = 47 | pages = 29407–10 | year = 1997 | pmid = 9367993 | doi = 10.1074/jbc.272.47.29407 }}
* {{cite journal | vauthors = Zumbrunn J, Trueb B | title = Assignment of the ZYX gene for the LIM protein zyxin to human chromosome bands 7q34→q35 by in situ hybridization | journal = Cytogenet. Cell Genet. | volume = 81 | issue = 3–4 | pages = 283–4 | year = 1998 | pmid = 9730620 | doi = 10.1159/000015047 }}
* {{cite journal | vauthors = Yang JX, Miao SY, Wu YW, Zhang Z, Zong SD, Wang LF, Koide SS | title = Gene encoding a human testis Sertoli cell component related to LIM domain protein | journal = Biochem. Mol. Biol. Int. | volume = 46 | issue = 1 | pages = 11–9 | year = 1998 | pmid = 9784834 | doi =  }}
* {{cite journal | vauthors = Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B | title = An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment | journal = J. Biol. Chem. | volume = 274 | issue = 19 | pages = 13410–8 | year = 1999 | pmid = 10224105 | doi = 10.1074/jbc.274.19.13410 }}
* {{cite journal | vauthors = Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM | title = Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins | journal = J. Biol. Chem. | volume = 275 | issue = 29 | pages = 22503–11 | year = 2000 | pmid = 10801818 | doi = 10.1074/jbc.M001698200 }}
* {{cite journal | vauthors = Hirota T, Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H | title = Zyxin, a Regulator of Actin Filament Assembly, Targets the Mitotic Apparatus by Interacting with H-Warts/Lats1 Tumor Suppressor | journal = J. Cell Biol. | volume = 149 | issue = 5 | pages = 1073–86 | year = 2000 | pmid = 10831611 | pmc = 2174824 | doi = 10.1083/jcb.149.5.1073 }}
* {{cite journal | vauthors = Smolenski A, Poller W, Walter U, Lohmann SM | title = Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I | journal = J. Biol. Chem. | volume = 275 | issue = 33 | pages = 25723–32 | year = 2000 | pmid = 10851246 | doi = 10.1074/jbc.M909632199 }}
* {{cite journal | vauthors = Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S | title = Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin | journal = J. Biol. Chem. | volume = 275 | issue = 40 | pages = 30817–25 | year = 2000 | pmid = 10882740 | doi = 10.1074/jbc.M005066200 }}
* {{cite journal | vauthors = Schenker T, Trueb B | title = BSPRY, a novel protein of the Ro-Ret family | journal = Biochim. Biophys. Acta | volume = 1493 | issue = 1–2 | pages = 255–8 | year = 2000 | pmid = 10978534 | doi = 10.1016/s0167-4781(00)00167-6 }}
* {{cite journal | vauthors = Li B, Trueb B | title = Analysis of the alpha-actinin/zyxin interaction | journal = J. Biol. Chem. | volume = 276 | issue = 36 | pages = 33328–35 | year = 2001 | pmid = 11423549 | doi = 10.1074/jbc.M100789200 }}
* {{cite journal | vauthors = Degenhardt YY, Silverstein S | title = Interaction of Zyxin, a Focal Adhesion Protein, with the E6 Protein from Human Papillomavirus Type 6 Results in Its Nuclear Translocation | journal = J. Virol. | volume = 75 | issue = 23 | pages = 11791–802 | year = 2001 | pmid = 11689660 | pmc = 114765 | doi = 10.1128/JVI.75.23.11791-11802.2001 }}
* {{cite journal | vauthors = Yi J, Kloeker S, Jensen CC, Bockholt S, Honda H, Hirai H, Beckerle MC | title = Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers | journal = J. Biol. Chem. | volume = 277 | issue = 11 | pages = 9580–9 | year = 2002 | pmid = 11782456 | doi = 10.1074/jbc.M106922200 }}
* {{cite journal | vauthors = van der Gaag EJ, Leccia MT, Dekker SK, Jalbert NL, Amodeo DM, Byers HR | title = Role of zyxin in differential cell spreading and proliferation of melanoma cells and melanocytes | journal = J. Invest. Dermatol. | volume = 118 | issue = 2 | pages = 246–54 | year = 2002 | pmid = 11841540 | doi = 10.1046/j.0022-202x.2001.01657.x }}
{{Refend}}
 
== External links ==
* [https://web.archive.org/web/20110722012353/http://cmkb.cellmigration.org/report.cgi?report=orth_overview&orth_acc=co00002107 Zyxin] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]
 
[[Category:Cytoskeleton]]

Latest revision as of 03:04, 19 September 2017

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

n/a

n/a

Ensembl

n/a

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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

Zyxin is a protein that in humans is encoded by the ZYX gene.[1][2][3]

Function

Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform.[3]

Interactions

Zyxin has been shown to interact with:

References

  1. ↑ Zumbrunn J, Trueb B (January 1997). "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts". Eur J Biochem. 241 (2): 657–63. doi:10.1111/j.1432-1033.1996.00657.x. PMID 8917469.
  2. ↑ Macalma T, Otte J, Hensler ME, Bockholt SM, Louis HA, Kalff-Suske M, Grzeschik KH, von der Ahe D, Beckerle MC (January 1997). "Molecular characterization of human zyxin". J Biol Chem. 271 (49): 31470–8. doi:10.1074/jbc.271.49.31470. PMID 8940160.
  3. ↑ 3.0 3.1 "Entrez Gene: ZYX zyxin".
  4. ↑ Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (May 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. PMID 10224105.
  5. ↑ Li B, Trueb B (September 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. doi:10.1074/jbc.M100789200. PMID 11423549.
  6. ↑ Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H, Shishido T (June 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. doi:10.1074/jbc.M301447200. PMID 12672821.
  7. ↑ 7.0 7.1 Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM (July 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. PMID 10801818.
  8. ↑ Li B, Zhuang L, Trueb B (May 2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. doi:10.1074/jbc.M310304200. PMID 15004028.
  9. ↑ Hirota T, Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H (May 2000). "Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor". J. Cell Biol. 149 (5): 1073–86. doi:10.1083/jcb.149.5.1073. PMC 2174824. PMID 10831611.
  10. ↑ Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.

Further reading

External links

Retrieved from "https://www.wikidoc.org/index.php?title=Zyxin&oldid=1421573"