AAA proteins

Current Opinion in Structural Biology

Volumn 12, Issue 6, 2002, Pages 746-753

  Lupas, Andrei N ^a   Martin, Jörg ^a  

^a MAX PLANCK INSTITUTE FOR DEVELOPMENTAL BIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEIN; PROTEIN AAA; UNCLASSIFIED DRUG;

BIODIVERSITY; ENZYME ACTIVITY; MOLECULAR BIOLOGY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW;

EID: 0036914160     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(02)00388-3     Document Type: Review

References (81)

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40. Ye Y., Meyer H.H., Rapoport T.A. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 414:2001;652-656. Three different groups (see also [41•,42•]) arrive at the same conclusion after studying the role of the AAA protein Cdc48 in yeast. This AAA protein is involved in the transport of proteins from the ER to the cytosol for subsequent degradation.
41. Jarosch E., Taxis C., Volkwein C., Bordallo J., Finley D., Wolf D.H., Sommer T. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol. 4:2002;134-139. See annotation to [40•].
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43. 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.
44. Titorenko V.I., Rachubinski R.A. Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p. J Cell Biol. 150:2000;881-886.
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66. Wu D., Chen P.J., Chen S., Hu Y., Nunez G., Ellis R.E. C. elegans MAC-1, an essential member of the AAA family of ATPases, can bind CED-4 and prevent cell death. Development. 126:1999;2021-2031.
67. Benaroudj N., Goldberg A.L. PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone. Nat Cell Biol. 2:2000;833-839. Proteases like to degrade unfolded proteins. As shown here and in two additional papers [68•,69•], proteasomes have an integrated unfoldase activity, consisting of AAA proteins at the base of the regulatory subcomplex.
68. Strickland E., Hakala K., Thomas P.J., DeMartino G.N. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome. J Biol Chem. 275:2000;5565-5572. See annotation to [67•].
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71. Thoms S. Cdc48 can distinguish between native and non-native proteins in the absence of cofactors. FEBS Lett. 520:2002;107-110.
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78. Horsnell W.G., Steel G.J., Morgan A. Analysis of NSF mutants reveals residues involved in SNAP binding and ATPase stimulation. Biochemistry. 41:2002;5230-5235.
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80. Chiba S., Akiyama Y., Ito K. Membrane protein degradation by FtsH can be initiated from either end. J Bacteriol. 184:2002;4775-4782. The first evidence that directionality in the translocation process of AAA ATPases is not determined by the orientation of the substrate polypeptide chain.
81. Krzywda S., Brzozowski A., Verma C., Karata K., Ogura T., Wilkinson A. The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 Å resolution. Structure. 10:2002;1073-1083.