TY - JOUR
T1 - ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome
AU - Kim, Young Chan
AU - Li, Xiaohua
AU - Thompson, David
AU - Demartino, George N.
PY - 2013/2/1
Y1 - 2013/2/1
N2 - Background: ATPase subunits mediate 26 S proteasome assembly and function. Results: Defective ATP binding by some ATPase subunits inhibits proteasome assembly, and proteasomes harboring an ATP binding-defective subunit are impaired for proteolysis, substrate-stimulated gating, and ATPase activity. Conclusion: The proteasome requires normal ATP binding for assembly and function. Significance: Protein substrates promote their own degradation by inducing ATP-dependent proteasome functions.
AB - Background: ATPase subunits mediate 26 S proteasome assembly and function. Results: Defective ATP binding by some ATPase subunits inhibits proteasome assembly, and proteasomes harboring an ATP binding-defective subunit are impaired for proteolysis, substrate-stimulated gating, and ATPase activity. Conclusion: The proteasome requires normal ATP binding for assembly and function. Significance: Protein substrates promote their own degradation by inducing ATP-dependent proteasome functions.
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U2 - 10.1074/jbc.M112.424788
DO - 10.1074/jbc.M112.424788
M3 - Article
C2 - 23212908
AN - SCOPUS:84873321806
SN - 0021-9258
VL - 288
SP - 3334
EP - 3345
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 5
ER -