原创力文档acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation乙酰化作用的胰岛素受体底物对酪氨酸磷酸化是宽容的.pdfVIP
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acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation乙酰化作用的胰岛素受体底物对酪氨酸磷酸化是宽容的
BMC Biology BioMed Central
Research article Open Access
Acetylation of insulin receptor substrate-1 is permissive for tyrosine
phosphorylation
Christina Kaiser and Stephen R James*
Address: Section of Cell Biology, Department of Biology, Biovitrum AB, SE-112 76, Stockholm, Sweden
Email: Christina Kaiser - christina.kaiser@; Stephen R James* - stephen.james@
* Corresponding author
Published: 02 November 2004 Received: 07 July 2004
Accepted: 02 November 2004
BMC Biology 2004, 2:23 doi:10.1186/1741-7007-2-23
This article is available from: /1741-7007/2/23
© 2004 Kaiser and James; licensee BioMed Central Ltd.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0),
which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
Background: Insulin receptor substrate (IRS) proteins are key moderators of insulin action. Their
specific regulation determines downstream protein-protein interactions and confers specificity on
growth factor signalling. Regulatory mechanisms that have been identified include phosphorylation
of IRS proteins on tyrosine and serine residues and ubiquitination of lysine residues. This study
investigated other potential molecular mechanisms of IRS-1 regulation.
Results: Using the sos recruitment yeast two-hybrid system we found that IRS-1 and histone
deacetylase 2 (HDAC2) interact in the cytoplasmic compartment
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