A human polymorphism affects NEDD4L subcellular targeting by leading to two isoforms that contain or lack a C2 domain |
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| Authors: | Nicholas F Garrone Bonnie L Blazer-Yost Robert B Weiss Jean-Marc Lalouel Andreas Rohrwasser |
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| Affiliation: | (1) Department of Human Genetics, Eccles Institute of Human Genetics, University of Utah School of Medicine, Salt Lake City, USA;(2) Department of Biology, Indiana University Purdue University at Indianapolis, Indianapolis, USA |
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| Abstract: | Background Ubiquitination serves multiple cellular functions, including proteasomal degradation and the control of stability, function, and intracellular localization of a wide variety of proteins. NEDD4L is a member of the HECT class of E3 ubiquitin ligases. A defining feature of NEDD4L protein isoforms is the presence or absence of an amino-terminal C2 domain, a class of subcellular, calcium-dependent targeting domains. We previously identified a common variant in human NEDD4L that generates isoforms that contain or lack a C2 domain. |
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