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Prepublished online as a Blood First Edition Paper on April 17, 2002; DOI 10.1182/blood-2001-11-0008. This Article Full Text Full Text (PDF) All Versions of this Article: 2001-11-0008v1 99/11/4219    most recent 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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Andrews, R. K. Articles by Berndt, M. C. Search for Related Content PubMed PubMed Citation Articles by Andrews, R. K. Articles by Berndt, M. C. Related Collections Hemostasis, Thrombosis, and Vascular Biology Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 June 2002, Vol. 99, No. 11, pp. 4219-4221 BRIEF REPORT Interaction of calmodulin with the cytoplasmic domain of platelet glycoprotein VI Robert K. Andrews, Katsue Suzuki-Inoue, Yang Shen, David Tulasne, Stephen P. Watson, and Michael C. Berndt From the Hazel and Pip Appel Vascular Biology Laboratory, Baker Medical Research Institute, Melbourne; the Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia; and the Department of Pharmacology, University of Oxford, United Kingdom. The platelet collagen receptor, glycoprotein VI (GPVI), and GPIb-IX-V, which binds von Willebrand factor, initiate platelet aggregation at low or high shear stress, respectively. We recently reported that positively charged, membrane-proximal sequences within cytoplasmic domains of GPIb and GPV of GPIb-IX-V bind calmodulin. We now show that GPVI also binds calmodulin as follows(1) calmodulin coimmunoprecipitated with GPVI from resting platelet lysates using an anti-GPVI IgG, but partially dissociated in platelets activated by collagen or collagen-related peptide; (2) calmodulin coprecipitated from platelet lysates with maltose-binding protein (MBP)-GPVI cytoplasmic domain fusion protein, but not MBP alone; (3) GPVI-related synthetic peptide based on the membrane-proximal sequence, His269-Pro287, induced a shift in calmodulin migration on nondenaturing gels, an assay that identifies calmodulin-binding peptides. His269-Pro287 is analogous to the calmodulin-binding sequence in GPIb. The novel interaction of GPVI and calmodulin may regulate aspects of GPVI function. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Z. W. Lai, R. A. Lew, M. A. Yarski, F.-T. Mu, R. K. Andrews, and A. I. Smith The Identification of a Calmodulin-Binding Domain within the Cytoplasmic Tail of Angiotensin-Converting Enzyme-2 Endocrinology, May 1, 2009; 150(5): 2376 - 2381. [Abstract] [Full Text] [PDF] E. E. Gardiner, D. Karunakaran, J. F. Arthur, F.-T. Mu, M. S. Powell, R. I. Baker, P. M. Hogarth, M. L. Kahn, R. K. Andrews, and M. C. Berndt Dual ITAM-mediated proteolytic pathways for irreversible inactivation of platelet receptors: de-ITAM-izing Fc{gamma}RIIa Blood, January 1, 2008; 111(1): 165 - 174. [Abstract] [Full Text] [PDF] J. F. Arthur, Y. Shen, M. L. Kahn, M. C. Berndt, R. K. Andrews, and E. E. 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