[HTML][HTML] The Lck SH3 domain negatively regulates localization to lipid rafts through an interaction with c-Cbl
IY Hawash, RL Geahlen, ML Harrison… - Journal of Biological …, 2002 - ASBMB
Lck is a member of the Src family of protein-tyrosine kinases and is essential for T cell
development and function. Lck is localized to the inner surface of the plasma membrane and
partitions into lipid rafts via dual acylation on its N terminus. We have tested the role of Lck
binding domains in regulating Lck localization to lipid rafts. A form of Lck containing a point
mutation inactivating the SH3 domain (W97ALck) was preferentially localized to lipid rafts
compared with wild type or SH2 domain-inactive (R154K) Lck when expressed in Lck …
development and function. Lck is localized to the inner surface of the plasma membrane and
partitions into lipid rafts via dual acylation on its N terminus. We have tested the role of Lck
binding domains in regulating Lck localization to lipid rafts. A form of Lck containing a point
mutation inactivating the SH3 domain (W97ALck) was preferentially localized to lipid rafts
compared with wild type or SH2 domain-inactive (R154K) Lck when expressed in Lck …