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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 (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 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 Social Bookmarking                   What's this? Submitted November 27, 2001 Accepted January 16, 2002 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 Vascular Biology Laboratory, Baker Medical Research Institute, Melbourne, VIC, Australia; Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, Australia Department of Pharmacology, University of Oxford, Oxford, United Kingdom * Corresponding author; email: rkandrews{at}hotmail.com. The platelet collagen receptor, glycoprotein (GP)VI, and GPIb-IX-V that 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 GPIbß and GPV of GPIb-IX-V bind calmodulin [Andrews RK, Munday AD, Mitchell CA, Berndt MC. Blood. 2001;98:681-687]. We now show that GPVI also binds calmodulin: (1) calmodulin co-immunoprecipitated 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 co-precipitated from platelet lysates with maltose-binding protein (MBP)-GPVI cytoplasmic domain fusion protein, but not MBP alone; (3) a GPVI-related synthetic peptide based on the membrane-proximal sequence, His269-Pro287, induced a shift in calmodulin migration on non-denaturing gels, an assay that identifies calmodulin-binding peptides. His269-Pro287 is analogous to the calmodulin-binding sequence in GPIbß. The novel interaction of GPVI and calmodulin may regulate aspects of GPVI function. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: E. Trifiro, S. A. Williams, Y. Cheli, K. Furihata, F. M. Pulcinelli, D. J. Nugent, and T. J. 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