HERC3 binding to and regulation by ubiquitin

FEBS Letters

Cruz, Cristina¹  Bartrons, Ramon¹  Ventura, Francesc¹  Rosa, Jose Luis¹ 

[1] Unitat de Bioquı́mica i Biologia Molecular, Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, C/Feixa Llarga s/n, E-08907 L'Hospitalet de Llobregat, Barcelona, Spain

关键词: HERC;    RCC1;    HECT;    E6 associated protein;    Intracellular transport;    Guanine nucleotide exchange;    HERC;    HECT domain and RCC1 domain protein;    HECT;    homologous to E6-AP carboxy-terminus;    E6-AP;    E6 associated protein;    RLD;    RCC1-like domain;   

DOI  :  10.1016/S0014-5793(00)02371-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Members of the HERC (domain homologous to E6 associated protein carboxy-terminus and RCC1 domain protein) family may function both as guanine nucleotide exchange factors and E3 ubiquitin ligases. Here we identify an unstudied member, HERC3. This protein was recognized by specific antibodies in different cell types. HERC3 was located in the cytosol and in vesicular-like structures containing β-COP, ARF and Rab5 proteins. Involvement of HERC3 in the ubiquitin system was suggested by its ability to interact with ubiquitin. The conserved cysteine in HECT proteins was not essential for this non-covalent binding. Moreover, HERC3 was a substrate of ubiquitination being degraded by the proteasome. These observations indicate a fine regulation of HERC3 and suggest a role in vesicular traffic and ubiquitin-dependent processes.

【 授权许可】

Unknown