PPP1R12B: Difference between revisions
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{{ | '''Protein phosphatase 1 regulatory subunit 12B''' is an [[enzyme]] that in humans is encoded by the ''PPP1R12B'' [[gene]].<ref name="pmid9570949">{{cite journal |vauthors=Fujioka M, Takahashi N, Odai H, Araki S, Ichikawa K, Feng J, Nakamura M, Kaibuchi K, Hartshorne DJ, Nakano T, Ito M | title = A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping | journal = Genomics | volume = 49 | issue = 1 | pages = 59–68 |date=Jun 1998 | pmid = 9570949 | pmc = | doi = 10.1006/geno.1998.5222 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4660| accessdate = }}</ref> | ||
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| summary_text = Myosin light chain phosphatase (MLCP) consists of three subunits- catalytic subunit, large subunit/myosin binding subunit (MBS) and small subunit (sm-M20). This gene is a multi-functional gene which encodes both MBS and sm-M20. MLCP regulates myosins and the dephosphorylation is enhanced by the presence of MBS. The sm-M20 is suggested to play a regulatory role in muscle contraction by binding to MBS. MBS is also encoded by another gene, myosin light chain phosphatase target subunit 1. sm-M20 shows higher binding affinity to this gene product than to myosin light chain phosphatase target subunit 2-MBS even though the two MBS proteins are highly similar. Although both MBSs increase the activity of MLCP, myosin light chain phosphatase target subunit 1-MBS is a more efficient activator. There are four alternatively spliced transcript variants described; two alter the MBS coding region and two alter the sm-M20 coding region of this gene.<ref name="entrez" | | summary_text = Myosin light chain phosphatase (MLCP) consists of three subunits- catalytic subunit, large subunit/myosin binding subunit (MBS) and small subunit (sm-M20). This gene is a multi-functional gene which encodes both MBS and sm-M20. MLCP regulates myosins and the dephosphorylation is enhanced by the presence of MBS. The sm-M20 is suggested to play a regulatory role in muscle contraction by binding to MBS. MBS is also encoded by another gene, myosin light chain phosphatase target subunit 1. sm-M20 shows higher binding affinity to this gene product than to myosin light chain phosphatase target subunit 2-MBS even though the two MBS proteins are highly similar. Although both MBSs increase the activity of MLCP, myosin light chain phosphatase target subunit 1-MBS is a more efficient activator. There are four alternatively spliced transcript variants described; two alter the MBS coding region and two alter the sm-M20 coding region of this gene.<ref name="entrez"/> | ||
}} | }} | ||
==Interactions== | |||
PPP1R12B has been shown to [[Protein-protein interaction|interact]] with [[Interleukin 16]].<ref name=pmid12923170>{{cite journal |last=Bannert |first=Norbert |authorlink= |author2=Vollhardt Karin |author3=Asomuddinov Bakhtier |author4=Haag Marion |author5=König Herbert |author6=Norley Stephen |author7=Kurth Reinhard |date=Oct 2003 |title=PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits |journal=J. Biol. Chem. |volume=278 |issue=43 |pages=42190–9 |publisher= |location = United States| issn = 0021-9258| pmid = 12923170 |doi = 10.1074/jbc.M306669200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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| citations = | | citations = | ||
*{{cite journal | | *{{cite journal |vauthors=Somlyo AP, Wu X, Walker LA, Somlyo AV |title=Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases. |journal=Rev. Physiol. Biochem. Pharmacol. |volume=134 |issue= |pages= 201–34 |year= 1999 |pmid= 10087910 |doi= 10.1007/3-540-64753-8_5}} | ||
*{{cite journal | author=Seki N | *{{cite journal | author=Seki N |title=Characterization of cDNA clones in size-fractionated cDNA libraries from human brain |journal=DNA Res. |volume=4 |issue= 5 |pages= 345–9 |year= 1998 |pmid= 9455484 |doi=10.1093/dnares/4.5.345 |name-list-format=vanc| author2=Ohira M | author3=Nagase T | display-authors=3 | last4=Ishikawa | first4=K | last5=Miyajima | first5=N | last6=Nakajima | first6=D | last7=Nomura | first7=N | last8=Ohara | first8=O }} | ||
*{{cite journal |vauthors=Moorhead G, Johnson D, Morrice N, Cohen P |title=The major myosin phosphatase in skeletal muscle is a complex between the beta-isoform of protein phosphatase 1 and the MYPT2 gene product |journal=FEBS Lett. |volume=438 |issue= 3 |pages= 141–4 |year= 1998 |pmid= 9827534 |doi=10.1016/S0014-5793(98)01276-9 }} | |||
*{{cite journal | | *{{cite journal | author=Somlyo AP |title=Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser |journal=J. Physiol. |volume=516 |issue= 3|pages= 630 |year= 1999 |pmid= 10200412 |doi=10.1111/j.1469-7793.1999.0630u.x | pmc=2269296 }} | ||
*{{cite journal | author=Somlyo AP |title=Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser | *{{cite journal | author=Arimura T |title=Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6073–82 |year= 2001 |pmid= 11067852 |doi= 10.1074/jbc.M008566200 |name-list-format=vanc| author2=Suematsu N | author3=Zhou YB | display-authors=3 | last4=Nishimura | first4=J | last5=Satoh | first5=S | last6=Takeshita | first6=A | last7=Kanaide | first7=H | last8=Kimura | first8=A }} | ||
*{{cite journal | author=Arimura T | *{{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 |bibcode=2002PNAS...9916899M}} | ||
*{{cite journal | author=Strausberg RL | *{{cite journal | author=Bannert N |title=PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42190–9 |year= 2004 |pmid= 12923170 |doi= 10.1074/jbc.M306669200 |name-list-format=vanc| author2=Vollhardt K | author3=Asomuddinov B | display-authors=3 | last4=Haag | first4=M | last5=König | first5=H | last6=Norley | first6=S | last7=Kurth | first7=R }} | ||
*{{cite journal | author=Bannert N | *{{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=Gerhard DS | *{{cite journal | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |name-list-format=vanc| author2=Venkatesan K | author3=Hao T | display-authors=3 | last4=Hirozane-Kishikawa | first4=Tomoko | last5=Dricot | first5=Amélie | last6=Li | first6=Ning | last7=Berriz | first7=Gabriel F. | last8=Gibbons | first8=Francis D. | last9=Dreze | first9=Matija |bibcode=2005Natur.437.1173R}} | ||
*{{cite journal | author=Rual JF | *{{cite journal | author=Okamoto R |title=Characterization and function of MYPT2, a target subunit of myosin phosphatase in heart |journal=Cell. Signal. |volume=18 |issue= 9 |pages= 1408–16 |year= 2007 |pmid= 16431080 |doi= 10.1016/j.cellsig.2005.11.001 |name-list-format=vanc| author2=Kato T | author3=Mizoguchi A | display-authors=3 | last4=Takahashi | first4=N | last5=Nakakuki | first5=T | last6=Mizutani | first6=H | last7=Isaka | first7=N | last8=Imanakayoshida | first8=K | last9=Kaibuchi | first9=K }} | ||
*{{cite journal | author=Okamoto R | *{{cite journal | author=Gregory SG |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |name-list-format=vanc| author2=Barlow KF | author3=McLay KE | display-authors=3 | last4=Kaul | first4=R. | last5=Swarbreck | first5=D. | last6=Dunham | first6=A. | last7=Scott | first7=C. E. | last8=Howe | first8=K. L. | last9=Woodfine | first9=K. |bibcode=2006Natur.441..315G}} | ||
*{{cite journal | author=Gregory SG | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
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Protein phosphatase 1 regulatory subunit 12B is an enzyme that in humans is encoded by the PPP1R12B gene.[1][2]
Myosin light chain phosphatase (MLCP) consists of three subunits- catalytic subunit, large subunit/myosin binding subunit (MBS) and small subunit (sm-M20). This gene is a multi-functional gene which encodes both MBS and sm-M20. MLCP regulates myosins and the dephosphorylation is enhanced by the presence of MBS. The sm-M20 is suggested to play a regulatory role in muscle contraction by binding to MBS. MBS is also encoded by another gene, myosin light chain phosphatase target subunit 1. sm-M20 shows higher binding affinity to this gene product than to myosin light chain phosphatase target subunit 2-MBS even though the two MBS proteins are highly similar. Although both MBSs increase the activity of MLCP, myosin light chain phosphatase target subunit 1-MBS is a more efficient activator. There are four alternatively spliced transcript variants described; two alter the MBS coding region and two alter the sm-M20 coding region of this gene.[2]
Interactions
PPP1R12B has been shown to interact with Interleukin 16.[3]
References
- ↑ Fujioka M, Takahashi N, Odai H, Araki S, Ichikawa K, Feng J, Nakamura M, Kaibuchi K, Hartshorne DJ, Nakano T, Ito M (Jun 1998). "A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping". Genomics. 49 (1): 59–68. doi:10.1006/geno.1998.5222. PMID 9570949.
- ↑ 2.0 2.1 "Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B".
- ↑ Bannert, Norbert; Vollhardt Karin; Asomuddinov Bakhtier; Haag Marion; König Herbert; Norley Stephen; Kurth Reinhard (Oct 2003). "PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits". J. Biol. Chem. United States. 278 (43): 42190–9. doi:10.1074/jbc.M306669200. ISSN 0021-9258. PMID 12923170.
Further reading
- Somlyo AP, Wu X, Walker LA, Somlyo AV (1999). "Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases". Rev. Physiol. Biochem. Pharmacol. 134: 201–34. doi:10.1007/3-540-64753-8_5. PMID 10087910.
- Seki N, Ohira M, Nagase T, et al. (1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Res. 4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID 9455484.
- Moorhead G, Johnson D, Morrice N, Cohen P (1998). "The major myosin phosphatase in skeletal muscle is a complex between the beta-isoform of protein phosphatase 1 and the MYPT2 gene product". FEBS Lett. 438 (3): 141–4. doi:10.1016/S0014-5793(98)01276-9. PMID 9827534.
- Somlyo AP (1999). "Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser". J. Physiol. 516 (3): 630. doi:10.1111/j.1469-7793.1999.0630u.x. PMC 2269296. PMID 10200412.
- Arimura T, Suematsu N, Zhou YB, et al. (2001). "Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit". J. Biol. Chem. 276 (9): 6073–82. doi:10.1074/jbc.M008566200. PMID 11067852.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Bannert N, Vollhardt K, Asomuddinov B, et al. (2004). "PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits". J. Biol. Chem. 278 (43): 42190–9. doi:10.1074/jbc.M306669200. PMID 12923170.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
- Okamoto R, Kato T, Mizoguchi A, et al. (2007). "Characterization and function of MYPT2, a target subunit of myosin phosphatase in heart". Cell. Signal. 18 (9): 1408–16. doi:10.1016/j.cellsig.2005.11.001. PMID 16431080.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
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