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PKCζII is a target for degradation through the tumour suppressor protein pVHL
Author(s) -
Iturrioz Xavier,
Parker Peter J.
Publication year - 2007
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/j.febslet.2007.02.059
Subject(s) - suppressor , degradation (telecommunications) , microbiology and biotechnology , chemistry , cancer research , protein kinase c , biophysics , biology , biochemistry , phosphorylation , computer science , gene , telecommunications
PKCζII is a rapidly degraded variant of PKCζ that suppresses epithelial cell polarisation. It is shown here that PKCζII is a target for the E3 ligase and tumour suppressor Von Hippel‐Lindau protein (pVHL). Deletion studies demonstrate that the C‐terminal region is required for the pVHL and proteasome dependent turnover of PKCζII, however it is the N‐terminal PB1 domain of PKCζII that is required for pVHL complex formation. Reciprocal deletion studies define the pVHL effector domain as the dominant PKCζII binding site. The results indicate that pVHL recruits PKCζII via its PB1 domain and causes ubiquitination and degradation via the distal C‐terminus of PKCζII.