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The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation

The negative regulator Cbl functions as a ubiquitin ligase towards activated receptor tyrosine kinases and facilitates their transport to lysosomes. Whether Cbl ubiquitin ligase activity mediates its negative regulatory effects on cytoplasmic tyrosine kinases of the Syk/ZAP‐70 family has not been ad...

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Published in:The EMBO journal 2001-12, Vol.20 (24), p.7085-7095
Main Authors: Rao, Navin, Ghosh, Amiya K., Ota, Satoshi, Zhou, Pengcheng, Reddi, Alagarsamy Lakku, Hakezi, Kaoru, Druker, Brian K., Wu, Jiong, Band, Hamid
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container_end_page 7095
container_issue 24
container_start_page 7085
container_title The EMBO journal
container_volume 20
creator Rao, Navin
Ghosh, Amiya K.
Ota, Satoshi
Zhou, Pengcheng
Reddi, Alagarsamy Lakku
Hakezi, Kaoru
Druker, Brian K.
Wu, Jiong
Band, Hamid
description The negative regulator Cbl functions as a ubiquitin ligase towards activated receptor tyrosine kinases and facilitates their transport to lysosomes. Whether Cbl ubiquitin ligase activity mediates its negative regulatory effects on cytoplasmic tyrosine kinases of the Syk/ZAP‐70 family has not been addressed, nor is it known whether these kinases are regulated via ubiquitylation during lymphocyte B‐cell receptor engagement. Here we show that B‐cell receptor stimulation in Ramos cells induces the ubiquitylation of Syk tyrosine kinase which is inhibited by a dominant‐negative mutant of Cbl. Intact tyrosine kinase‐binding and RING finger domains of Cbl were found to be essential for Syk ubiquitylation in 293T cells and for in vitro Syk ubiquitylation. These same domains were also essential for Cbl‐mediated negative regulation of Syk as measured using an NFAT‐luciferase reporter in a lymphoid cell. Association with Cbl did not alter the kinase activity of Syk. Altogether, our results support an essential role for Cbl ubiquitin ligase activity in the negative regulation of Syk, and establish that ubiquitylation provides a mechanism of Cbl‐mediated negative regulation of cytoplasmic targets.
doi_str_mv 10.1093/emboj/20.24.7085
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identifier ISSN: 0261-4189
ispartof The EMBO journal, 2001-12, Vol.20 (24), p.7085-7095
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1460-2075
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subjects activation
Cell Line
Cysteine Endopeptidases - drug effects
Cysteine Proteinase Inhibitors - pharmacology
Enzyme Precursors - metabolism
Humans
Intracellular Signaling Peptides and Proteins
lymphocyte
Lymphocytes
Multienzyme Complexes - drug effects
Oncogene Protein v-cbl
Proteasome Endopeptidase Complex
Protein-Tyrosine Kinases - metabolism
Receptors, Antigen, B-Cell - metabolism
Recombinant Proteins - metabolism
regulation
Retroviridae Proteins, Oncogenic - metabolism
Syk Kinase
Syk protein
tyrosine kinase
Ubiquitin - metabolism
ubiquitylation
ZAP-70 protein
title The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation
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