HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 32, 28934-28941, August 9, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/32/28934    most recent M204340200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kato, A. Articles by Oshimi, K. Search for Related Content PubMed PubMed Citation Articles by Kato, A. Articles by Oshimi, K. Social Bookmarking                      What's this?

Ancient Ubiquitous Protein 1 Binds to the Conserved Membrane-proximal Sequence of the Cytoplasmic Tail of the Integrin  Subunits That Plays a Crucial Role in the Inside-out Signaling of _IIb3^*

Atsushi Kato^§, Norihiko Kawamata, Kenji Tamayose, Motoki Egashira, Rika Miura, Tsutomu Fujimura^¶, Kimie Murayama^¶, and Kazuo Oshimi

From the  Division of Hematology, Department of Internal Medicine and ^¶ Division of Biochemical Analysis, Central Laboratory of Medical Sciences, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

Modification of the cytoplasmic tails of the integrin _IIb3 plays an important role in the signal transduction in platelets. We searched for proteins that bind to the _IIb cytoplasmic tail using the yeast two-hybrid assay with a cDNA library of the megakaryocyte-derived cell line and identified a protein, ancient ubiquitous protein 1 (Aup1), that is ubiquitously expressed in human cells. Observation of UT7/TPO cells expressing a red fluorescent protein-tagged Aup1 indicated its localization in the cytoplasm. Immunoprecipitation of UT7/TPO cells by an antibody for Aup1 revealed that ~40% of _IIb is complexed with Aup1. Binding study with an _IIb cytoplasmic tail peptide and glutathione S-transferase-Aup1 fusion protein revealed a low affinity (K_d = 90 µM). Subsequent yeast two-hybrid assay indicated binding of Aup1 to cytoplasmic tails of other integrin  subunits. Binding study with the purified Aup1 and various glutathione S-transferase-_IIb cytoplasmic tail peptides revealed specific binding of Aup1 to the membrane-proximal sequence (KVGFFKR) that is conserved among the integrin  subunits and plays a crucial role in the _IIb3 inside-out signaling. As Aup1 possesses domains related to signal transduction, these results suggest involvement of Aup1 in the integrin signaling.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				J. J. Calvete Structures of Integrin Domains and Concerted Conformational Changes in the Bidirectional Signaling Mechanism of {alpha}IIb{beta}3 Experimental Biology and Medicine, September 1, 2004; 229(8): 732 - 744. [Abstract] [Full Text] [PDF]

				D. Larkin, D. Murphy, D. F. Reilly, M. Cahill, E. Sattler, P. Harriott, D. J. Cahill, and N. Moran ICln, a Novel Integrin {alpha}IIb{beta}3-Associated Protein, Functionally Regulates Platelet Activation J. Biol. Chem., June 25, 2004; 279(26): 27286 - 27293. [Abstract] [Full Text] [PDF]