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XB-ART-45552
PLoS One January 1, 2012; 7 (6): e39505.
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Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.

Kalinichenko SV , Itoh K , Korobko EV , Sokol SY , Buchman VL , Korobko IV .


Abstract
MAK-V/Hunk is a scantily characterized AMPK-like protein kinase. Recent findings identified MAK-V as a pro-survival and anti-apoptotic protein and revealed its role in embryonic development as well as in tumorigenesis and metastasis. However molecular mechanisms of MAK-V action and regulation of its activity remain largely unknown. We identified Nedd4 as an interaction partner for MAK-V protein kinase. However, this HECT-type E3 ubiquitin ligase is not involved in the control of MAK-V degradation by the ubiquitin-proteasome system that regulates MAK-V abundance in cells. However, Nedd4 in an ubiquitin ligase-independent manner rescued developmental defects in Xenopus embryos induced by MAK-V overexpression, suggesting physiological relevance of interaction between MAK-V and Nedd4. This identifies Nedd4 as the first known regulator of MAK-V function.

PubMed ID: 22745772
PMC ID: PMC3379983
Article link: PLoS One
Grant support: [+]

Species referenced: Xenopus
Genes referenced: hunk mak myc nedd4 prkaa1
Antibodies: FLAG Ab2 Hunk Ab1 Nedd4l Ab1 Tuba4b Ab2


Article Images: [+] show captions
References [+] :
Buchman, Organization of the mouse Ruk locus and expression of isoforms in mouse tissues. 2002, Pubmed