Platelet adhesion: Structural and functional diversity of short dystrophin and utrophins in the formation of dystrophinassociated-protein complexes related to actin dynamics

Cerecedo, Doris; Martínez-Rojas, Dalila; Chávez, O scar; Martínez-Pérez, Francisco; Garcı́a-Sierra, Francisco; Rendón, Álvaro; Mornet, Dominique; Mondragón, Ricardo

doi:10.1160/th04-11-0765

Cited by 21 publications

(27 citation statements)

References 47 publications

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“…Two alternative DAPC-like complexes were identified by confocal microscope and by immunoprecipitation analyses in both platelets [48] and neutrophils [49], which were composed of Dp71d or Dp71 Δ110 , and β-dystroglycan, α-syntrophin, and α-dystrobrevin-1 and −2. These complexes were found associated with the actin-based cytoskeleton in neutrophils, likely by the interaction of actin with the actinbinding motifs present in Dp71.…”

Section: Formation and Distribution Of The Dp71-containing Dystrophinmentioning

confidence: 99%

Dystrophin Dp71: The Smallest but Multifunctional Product of the Duchenne Muscular Dystrophy Gene

et al. 2011

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Dystrophin Dp71 is expressed in all tissues, with the exception of skeletal muscle, and is the main Duchenne muscular dystrophy (DMD) gene product in brain. As full-length dystrophin does in skeletal muscle, Dp71 associates with dystroglycans, sarcoglycans, dystrobrevins, syntrophins, and accessory proteins to form the dystrophin-associated protein complex (DAPC) in non-muscle tissues. Although it has been nearly 20 years since the discovery of Dp71, its study has become relevant only recently due to its direct involvement with the two main DMD non-muscular phenotypes: cognitive impairment and abnormal retinal physiology. In this review, we describe the historical background of Dp71 and the experimental models developed for its study. Additionally, we present and discuss the experimental evidence supporting the participation of Dp71 in different cellular processes, including cell adhesion, water homeostasis, cell division, and nuclear architecture. The functional diversity of Dp71 is attributed to the formation of Dp71-containing DAPC in numerous cell types and different subcellular compartments, including in plasma membrane and nucleus, as well as to the capability of Dp71-containing DAPC to work as the scaffold for proper clustering and anchoring of structural and signaling proteins to the plasma membrane and of nuclear envelope proteins to the inner nuclear membrane.

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Section: Formation and Distribution Of The Dp71-containing Dystrophinmentioning

confidence: 99%

Dystrophin Dp71: The Smallest but Multifunctional Product of the Duchenne Muscular Dystrophy Gene

et al. 2011

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“…Dystrophin and utrophin gene products are associated with proteins, such as dystroglycans, sarcoglycans, dystrobrevins, and syntrophins, forming the named dystrophin-associated protein complex (DAPC) (Cox et al, 1994;Greenberg et al, 1994). Recently, the presence of the DAPC corresponding to Dp71d and Dp71D 110 isoforms, and utrophin gene products Up400 and Up71, which participate in shape changes, adhesion process and aggregation, was demonstrated in human platelets (Cerecedo et al, 2005).…”

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confidence: 99%

Role of dystrophins and utrophins in platelet adhesion process

et al. 2006

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SummaryPlatelets are crucial at the site of vascular injury, adhering to the sub‐endothelial matrix through receptors on their surface, leading to cell activation and aggregation to form a haemostatic plug. Platelets display focal adhesions as well as stress fibres to contract and facilitate expulsion of growth and pro‐coagulant factors contained in the granules and to constrict the clot. The interaction of F‐actin with different actin‐binding proteins determines the properties and composition of the focal adhesions. Recently, we demonstrated the presence of dystrophin‐associated protein complex corresponding to short dystrophin isoforms (Dp71d and Dp71) and the uthophin gene family (Up400 and Up71), which promote shape change, adhesion, aggregation, and granule centralisation. To elucidate participation of both complexes during the platelet adhesion process, their potential association with integrin β‐1 fraction and the focal adhesion system (α‐actinin, vinculin and talin) was evaluated by immunofluorescence and immunoprecipitation assays. It was shown that the short dystrophin‐associated protein complex participated in stress fibre assembly and in centralisation of cytoplasmic granules, while the utrophin‐associated protein complex assembled and regulated focal adhesions. The simultaneous presence of dystrophin and utrophin complexes indicates complementary structural and signalling mechanisms to the actin network, improving the platelet haemostatic role.

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“…In 1995, utrophin was described as a component of the platelet cytoskeleton, participating in its reorganization [28], while in hematopoietic stem/progenitor cells, Up400 and Up140 comprised the main gene products [29]. In addition, Up71 has been described in platelets [30], as well as in neutrophils [31].…”

Section: Dystrophin-related Proteinsmentioning

confidence: 99%

“…They were probably involved in deining platelet shape, substrate adhesion, and granule migration, as well as possessing a signaling role, participating in signaling triggered by adhesion to glass and by interaction with agonists such as thrombin [30].…”

Section: Dual Role Of the Dp71 Isoformmentioning

confidence: 99%

Dystrophin–Glycoprotein Complex in Blood Cells

Cerecedo¹

2017

Cytoskeleton - Structure, Dynamics, Function and Disease

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The Dystrophin-Associated Protein Complex (DAPC), known as the DystrophinGlycoprotein Complex (DGC), comprises an array of glycoproteins that are essential for the normal function of striated muscle, in which they were irst described, and for many other tissues, including blood. Understanding the role that these molecules play in muscle function has increased over the last decade, and some of the knowledge derived can be applied to other biological systems. However, there is no doubt that to date, some progress has been achieved in blood cells. Multiple interactions have been described among the proteins comprising the DGC, it is now well established that the DGC possesses a crucial role for numerous signaling pathways, recruiting and regulating various signaling proteins into a macromolecular complex. The aim of this chapter is to summarize the current state of knowledge regarding DGC processing and assembly, mainly in muscle tissue and in blood cells, with a primary focus on the dystroglycan heterodimer and associated proteins, including ion channels and membrane lipids. In addition, and due to increasing evidence involving dystroglycan proteins in the pathophysiology of solid tissue cancer, Duchenne muscular dystrophy, and leukemia, current information on these topics will be included.

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Platelet adhesion: Structural and functional diversity of short dystrophin and utrophins in the formation of dystrophinassociated-protein complexes related to actin dynamics

Cited by 21 publications

References 47 publications

Dystrophin Dp71: The Smallest but Multifunctional Product of the Duchenne Muscular Dystrophy Gene

Dystrophin Dp71: The Smallest but Multifunctional Product of the Duchenne Muscular Dystrophy Gene

Role of dystrophins and utrophins in platelet adhesion process

Dystrophin–Glycoprotein Complex in Blood Cells

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