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The human stress-activated protein kinase-interacting 1 gene encodes JNK-binding proteins.

Abstract：

:The orthologous proteins of the stress-activated protein kinase-interacting 1 (Sin1) family have been implicated in several different signal transduction pathways. In this study, we have investigated the function of the full-length human Sin1 protein and a C-terminally truncated isoform, Sin1alpha, which is produced by alternative splicing. Immunoblot analysis using an anti-Sin1 polyclonal antibody showed that full-length Sin1 and several smaller isoforms are widely expressed. Sin1 was demonstrated to bind to c-Jun N-terminal kinase (JNK) in vitro and in vivo, while no interaction with p38- or ERK1/2-family MAPKs was observed. The Sin1alpha isoform could also form a complex with JNK in vivo. Despite localizing in distinct compartments within the cell, both Sin1 and Sin1alpha co-localized with JNK, suggesting that the Sin1 proteins could recruit JNK. Over-expression of full-length Sin1 inhibited the activation of JNK by UV-C in DG75 cells, as well as basal JNK-activity in HEK293 cells. These data suggest that the human Sin1 proteins may act as scaffold molecules in the regulation of signaling by JNK.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Schroder W,Bushell G,Sculley T

doi

10.1016/j.cellsig.2004.10.015

subject

Has Abstract

pub_date

2005-06-01 00:00:00

pages

761-7

issue

6

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(04)00236-0

journal_volume

17

pub_type

杂志文章

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