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HERC3 binding to and regulation by ubiquitin
Author(s) -
Cruz Cristina,
Ventura Francesc,
Bartrons Ramon,
Rosa Jose Luis
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02371-1
Subject(s) - ubiquitin , guanine nucleotide exchange factor , proteasome , microbiology and biotechnology , deubiquitinating enzyme , biochemistry , chemistry , f box protein , cytosol , function (biology) , ubiquitin ligase , biology , enzyme , signal transduction , gene
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.