Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities

Biochemical and Biophysical Research Communications

Volumn 300, Issue 2, 2003, Pages 253-260

  Wang, Qing ^a   Song, Changcheng ^b   Li, Chou Chi H ^b  

^a NATIONAL CANCER INSTITUTE   (United States)

^b SAIC FREDERICK INC   (United States)

Author keywords

ATP binding; ATPase; Hexamerization; p97 VCP; Ubiquitin proteasome degradation

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; MUTANT PROTEIN; PROTEASOME; PROTEIN P97; UBIQUITIN; UNCLASSIFIED DRUG; UREA; VALOSIN CONTAINING PROTEIN; CDC48 PROTEIN; CELL CYCLE PROTEIN; CYSTEINE PROTEINASE; MULTIENZYME COMPLEX; PROTEIN SUBUNIT;

ARTICLE; BINDING SITE; CHEMICAL REACTION; DISSOCIATION; ENZYME ACTIVITY; HEXAMERIZATION; HYBRID; KINETICS; MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; WILD TYPE; ANIMAL; CHEMISTRY; METABOLISM; PHYSIOLOGY; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CELL CYCLE PROTEINS; CYSTEINE ENDOPEPTIDASES; KINETICS; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; STRUCTURE-ACTIVITY RELATIONSHIP; UBIQUITIN; UREA;

EID: 0037427531     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02840-1     Document Type: Article

References (26)

1. Neuwald A.F., Aravind L., Spouge J.L., Koonin E.V. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:1999;27-43.
2. Ogura T., Wilkinson A.J. AAA+ superfamily ATPases: common structure-diverse function. Genes Cells. 6:2001;575-597.
3. Maurizi M.R., Li C.C. AAA proteins: in search of a common molecular basis: International meeting on cellular functions of AAA proteins. EMBO Rep. 2:2001;980-985.
4. Vale R.D. AAA proteins. Lords of the ring. J. Cell Biol. 150:2000;F13-F19.
5. Patel S., Latterich M. The AAA team: related ATPases with diverse functions. Trends Cell Biol. 8:1998;65-71.
6. Zwickl P., Baumeister W. AAA-ATPases at the crossroads of protein life and death. Nat. Cell Biol. 1:1999;E97-98.
7. Confalonieri F., Duguet M. A 200-amino acid ATPase module in search of a basic function. Bioessays. 17:1995;639-650.
8. Peters J.M., Harris J.R., Lustig A., Muller S., Engel A., Volker S., Franke W.W. Ubiquitous soluble Mg (2+)-ATPase complex. A structural study. J. Mol. Biol. 223:1992;557-571.
9. Rouiller I., Butel V.M., Latterich M., Milligan R.A., Wilson-Kubalek E.M. A major conformational change in p97 AAA ATPase upon ATP binding. Mol. Cell. 6:2000;1485-1490.
10. Zhang X., Shaw A., Bates P.A., Newman R.H., Gowen B., Orlova E., Gorman M.A., Kondo H., Dokurno P., Lally J., Leonard G., Meyer H., van Heel M., Freemont P.S. Structure of the AAA ATPase p97. Mol. Cell. 6:2000;1473-1484.
11. Dai R.M., Li C.C. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 3:2001;740-744.
12. Lissin N.M., Venyaminov S., Girshovich A.S. (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL. Nature. 348:1990;339-342.
13. Dai R.M., Chen E., Longo D.L., Gorbea C.M., Li C.C. Involvement of valosin-containing protein, an ATPase Co-purified with I. κ B α and 26S proteasome, in ubiquitin-proteasome-mediated degradation of I κ B α J. Biol. Chem. 273:1998;3562-3573.
14. Lanzetta P.A., Alvarez L.J., Reinach P.S., Candia O.A. An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100:1979;95-97.
15. Cogan E.B., Birrell G.B., Griffith O.H. A robotics-based automated assay for inorganic and organic phosphates. Anal. Biochem. 271:1999;29-35.
16. Beckwith M., Longo D.L., O'Connell C.D., Moratz C.M., Urba W.J. Phorbol ester-induced, cell-cycle-specific, growth inhibition of human B-lymphoma cell lines. J. Natl. Cancer Inst. 82:1990;501-509.
17. Privalov P.L., Gill S.J. Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39:1988;191-234.
18. Egerton M., Ashe O.R., Chen D., Druker B.J., Burgess W.H., Samelson L.E. VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. EMBO J. 11:1992;3533-3540.
19. Seol J.H., Baek S.H., Kang M.S., Ha D.B., Chung C.H. Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli. J. Biol. Chem. 270:1995;8087-8092.
20. Singh S.K., Maurizi M.R. Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli. J. Biol. Chem. 269:1994;29537-29545.
21. Watanabe Y.H., Motohashi K., Yoshida M. Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J. Biol. Chem. 277:2002;5804-5809.
22. Nagiec E.E., Bernstein A., Whiteheart S.W. Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem. 270:1995;29182-29188.
23. Whiteheart S.W., Rossnagel K., Buhrow S.A., Brunner M., Jaenicke R., Rothman J.E. N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126:1994;945-954.
24. Parsell D.A., Kowal A.S., Lindquist S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J. Biol. Chem. 269:1994;4480-4487.
25. Schirmer E.C., Ware D.M., Queitsch C., Kowal A.S., Lindquist S.L. Subunit interactions influence the biochemical and biological properties of Hsp104. Proc. Natl. Acad. Sci. USA. 98:2001;914-919.
26. Lamb J.R., Fu V., Wirtz E., Bangs J.D. Functional analysis of the trypanosomal AAA protein TbVCP with trans-dominant ATP hydrolysis mutants. J. Biol. Chem. 276:2001;21512-21520.