Is an ATPase involved in uncoating of plasma membrane adaptor complex AP‐2?

FEBS Letters

von Figura, Kurt¹  Sosa, Miguel A²  Hille-Rehfeld, Annette¹  Bertini, Francisco² 

[1] Georg August Universität Göttingen, Zentrum für Biochemie und Molekulare Zellbiologie, Abt. Biochemie II, Gosslerstr. 12d, 37073 Göttingen, Germany;Instituto de Histologia y Embriologia, Facultad de Ciencias Médicas, Universidad Nacional de Cuyo, Casilla de Correo 56, 5500 Mendoza, Argentina

关键词: ATPase;    Plasma membrane adaptor complex;    Adaptin-2;    AP;    adaptin;    ATP-γ-S;    adenosine 5′-O-(3-thiotriphosphate);    GTP-γ-S;    guanosine 5′-O-(3-thiotriphosphate);    Hsc70;    70 kDa heat shock cognate protein;    TGN;    trans Golgi network;   

DOI  :  10.1016/S0014-5793(97)00331-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The coat of clathrin-coated vesicles mostly consists of clathrin and adaptor complexes AP-1 or AP-2. Clathrin is released from the vesicles in an ATP-dependent fashion prior to their fusion with endosomes. In the present study we found that ATP strongly inhibits in vitro binding of cytosolic AP-2 to membranes of stripped vesicles, and promotes the release of endogenous AP-2 from clathrin-deprived coated vesicles. Both effects required hydrolysis of ATP. In contrast, binding of AP-1 to stripped vesicles was not affected by ATP, but was enhanced by GTP-γ-S. These results point to an ATPase that promotes the release of AP-2 from clathrin-coated vesicles.

【 授权许可】

Unknown