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Anti-IgM induces up-regulation and tyrosine-phosphorylation of heterogeneous nuclear ribonucleoprotein K proteins (hnRNP K) in a Ramos B cell line.

Authors
 Hye-Kyung Jeon  ;  Jeong-Hun Ahn  ;  Jongseon Choe  ;  Jeon Han Park  ;  Tae H. Lee 
Citation
 IMMUNOLOGY LETTERS, Vol.98(2) : 303-310, 2005 
Journal Title
 IMMUNOLOGY LETTERS 
ISSN
 0165-2478 
Issue Date
2005
Abstract
Heterogeneous nuclear ribonucleoprotein K protein (hnRNP K) has diverse molecular partners implicated in signal transduction pathways, and is tyrosine-phosphorylated in response to growth factors and oxidative stress. Among the structurally distinct domains of hnRNP K, an SH3-binding domain (SH3BD) has been known to promote the association of SH3-containing tyrosine kinases and protooncoprotein Vav, which are involved in B cell receptor (BCR) signalling. In this study, we analyzed proteins of Ramos B cell line that are altered upon BCR activation with anti-IgM antibody, revealing that a certain hnRNP K isoform is up-regulated in response to anti-IgM treatment. We also showed that hnRNP K is tyrosine-phosphorylated after BCR ligation. HnRNP K lacking the SH3BD is shown not to interact with phosphorylated Vav, and Ramos cells stably expressing this mutant protein are less susceptible to anti-IgM-induced apoptosis, indicating that hnRNP K is coupled to BCR-mediated signalling and its SH3BD is required for proper signal propagation. Our results provide the first evidence that hnRNP K is involved in BCR signalling pathway.
DOI
10.1016/j.imlet.2004.12.005
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Park, Jeon Han(박전한) ORCID logo https://orcid.org/0000-0001-9604-3205
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/165733
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