POSH2 is a RING finger E3 ligase with Rac1 binding activity through a partial CRIB domain

FEBS Letters

Volumn 584, Issue 18, 2010, Pages 3867-3872

  Kärkkäinen, Satu ^a   van der Linden, Maarten ^a   Renkema, G Herma ^a,b,c  

^a UNIVERSITY OF TAMPERE   (Finland)

^b TAMPERE UNIVERSITY HOSPITAL   (Finland)

^c NONE   (Finland)

Author keywords

CRIB domain; E3 ligase; P21 Activated kinase; Plenty of SH3 domains; Src homology 3

Indexed keywords

GUANOSINE TRIPHOSPHATE; P21 ACTIVATED KINASE 2; PROTEIN CDC42; PROTEIN POSH2; PROTEIN SH3; RAC1 PROTEIN; RING FINGER PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; POSH2 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; RING FINGER MOTIF;

AMINO ACID SEQUENCE; CDC42 GTP-BINDING PROTEIN; HUMANS; MOLECULAR SEQUENCE DATA; RAC1 GTP-BINDING PROTEIN; RING FINGER DOMAINS; UBIQUITIN-PROTEIN LIGASES;

MAMMALIA;

EID: 77956916650     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.07.060     Document Type: Article

References (25)

1. Mayer B.J., Hamaguchi M., Hanafusa H. A novel viral oncogene with structural similarity to phospholipase C. Nature 1988, 332:272-275.
2. Stahl M.L., Ferenz C.R., Kelleher K.L., Kriz R.W., Knopf J.L. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature 1988, 332:269-272.
3. Karkkainen S., Hiipakka M., Wang J.H., Kleino I., Vaha-Jaakkola M., Renkema G.H., Liss M., Wagner R., Saksela K. Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome. EMBO Rep. 2006, 7:186-191.
4. Mayer B.J., Eck M.J. SH3 domains. Minding your p's and q's. Curr. Biol. 1995, 5:364-367.
5. Bokoch G.M. Biology of the p21-activated kinases. Annu. Rev. Biochem. 2003, 72:743-781.
6. Szczepanowska J. Involvement of Rac/Cdc42/PAK pathway in cytoskeletal rearrangements. Acta Biochim. Pol. 2009, 56:225-234.
7. Pacheco A., Chernoff J. Group I p21-activated kinases: emerging roles in immune function and viral pathogenesis. Int. J. Biochem. Cell Biol. 2010, 42:13-16.
8. Chang Y.W., Bean R.R., Jakobi R. Targeting RhoA/Rho kinase and p21-activated kinase signaling to prevent cancer development and progression. Recent Pat. Anticancer Drug Discov. 2009, 4:110-124.
9. Vadlamudi R.K., Kumar R. P21-activated kinase 1: an emerging therapeutic target. Cancer Treat. Res. 2004, 119:77-88.
10. Parrini M.C., Lei M., Harrison S.C., Mayer B.J. Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1. Mol. Cell 2002, 9:73-83.
11. Tapon N., Nagata K., Lamarche N., Hall A. A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways. EMBO J. 1998, 17:1395-1404.
12. Wilhelm M., Kukekov N.V., Xu Z., Greene L.A. Identification of POSH2, a novel homologue of the c-Jun N-terminal kinase scaffold protein POSH. Dev. Neurosci. 2007, 29:355-362.
13. Xu Z., Kukekov N.V., Greene L.A. POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis. EMBO J. 2003, 22:252-261.
14. Heikkinen L.S., Kazlauskas A., Melen K., Wagner R., Ziegler T., Julkunen I., Saksela K. Avian and 1918 Spanish influenza a virus NS1 proteins bind to Crk/CrkL Src homology 3 domains to activate host cell signaling. J. Biol. Chem. 2008, 283:5719-5727.
15. Manninen A., Hiipakka M., Vihinen M., Lu W., Mayer B.J., Saksela K. SH3-domain binding function of HIV-1 Nef is required for association with a PAK-related kinase. Virology 1998, 250:273-282.
16. Renkema G.H., Manninen A., Saksela K. Human immunodeficiency virus type 1 Nef selectively associates with a catalytically active subpopulation of p21-activated kinase 2 (PAK2) independently of PAK2 binding to Nck or beta-PIX. J. Virol. 2001, 75:2154-2160.
17. Manninen A., Renkema G.H., Saksela K. Synergistic activation of NFAT by HIV-1 nef and the Ras/MAPK pathway. J. Biol. Chem. 2000, 275:16513-16517.
18. Votteler J., Iavnilovitch E., Fingrut O., Shemesh V., Taglicht D., Erez O., Sorgel S., Walther T., Bannert N., Schubert U., Reiss Y. Exploring the functional interaction between POSH and ALIX and the relevance to HIV-1 release. BMC Biochem. 2009, 10:12.
19. Burbelo P.D., Drechsel D., Hall A. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 1995, 270:29071-29074.
20. Zhao Z.S., Manser E., Chen X.Q., Chong C., Leung T., Lim L. A conserved negative regulatory region in alpha PAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1. Mol. Cell. Biol. 1998, 18:2153-2163.
21. Xu Z., Greene L.A. Activation of the apoptotic JNK pathway through the Rac1-binding scaffold protein POSH. Methods Enzymol. 2006, 406:479-489.
22. Joberty G., Petersen C., Gao L., Macara I.G. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2000, 2:531-539.
23. Garrard S.M., Capaldo C.T., Gao L., Rosen M.K., Macara I.G., Tomchick D.R. Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6. EMBO J. 2003, 22:1125-1133.
24. Lyons T.R., Thorburn J., Ryan P.W., Thorburn A., Anderson S.M., Kassenbrock C.K. Regulation of the Pro-apoptotic scaffolding protein POSH by Akt. J. Biol. Chem. 2007, 282:21987-21997.
25. Seong K.H., Matsuo T., Fuyama Y., Aigaki T. Neural-specific overexpression of drosophila plenty of SH3s (DPOSH) extends the longevity of adult flies. Biogerontology 2001, 2:271-281.