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β‐Dystroglycan modulates the interplay between actin and microtubules in human‐adhered platelets
Author(s) -
Cerecedo Doris,
Cisneros Bulmaro,
SuárezSánchez Rocío,
HernándezGonzález Enrique,
Galván Iván
Publication year - 2008
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.2008.07048.x
Subject(s) - microbiology and biotechnology , cytoskeleton , microtubule , focal adhesion , microfilament , actin , actin cytoskeleton , filamin , biology , chemistry , signal transduction , biochemistry , cell
Summary To maintain the continuity of an injured blood vessel, platelets change shape, secrete granule contents, adhere, aggregate, and retract in a haemostatic plug. Ordered arrays of microtubules, microfilaments, and associated proteins are responsible for these platelet responses. In full‐spread platelets, microfilament bundles in association with other cytoskeleton proteins are anchored in focal contacts. Recent studies in migrating cells suggest that co‐ordination and direct physical interaction of microtubules and actin network modulate adhesion development. In platelets, we have proposed a feasible association between these two cytoskeletal systems, as well as the participation of the dystrophin‐associated protein complex, as part of the focal adhesion complex. The present study analysed the participation of microtubules and actin during the platelet adhesion process. Confocal microscopy, fluorescence resonance transfer energy and immunoprecipitation assays were used to provide evidence of a cross‐talk between these two cytoskeletal systems. Interestingly, β‐dystroglycan was found to act as an interplay protein between actin and microtubules and an additional communication between these two cytoskeleton networks was maintained through proteins of focal adhesion complex. Altogether our data are indicative of a dynamic co‐participation of actin filaments and microtubules in modulating focal contacts to achieve platelet function.