Neuron
ArticleThe 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin
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Phosphorylation of a-dystrobrevin is essential for akap accumulation and acetylcholine receptor stability
2020, Journal of Biological ChemistryRole of α-Dystrobrevin in the differentiation process of HL-60 cells
2018, Experimental Cell ResearchCitation Excerpt :Therefore, we corroborated that the relative immunofluorescence of actin-F was higher for α-Db-depleted differentiated HL-60 cells than for their controls (Fig. 5, Panel D). Neutrophils derived from HL-60 cells display functions similar to those of blood neutrophils in response to chemotactic gradients [28], such as phagocytosis, migration to the site-of-infection and eliminating bacteria [1,2]. During this process, the neutrophils depend on the actin rearrangements of their actin cytoskeletons, extending actin-rich pseudopodia in response to chemotactic gradients [29].
Dystrophin complex functions as a scaffold for signalling proteins
2014, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :The SU domain and PH-2 domain interact with the carboxy terminus of dystrophin [95,96]. There are two syntrophin binding sites in the carboxy terminus of dystrophin and additional two sites on α-dystrobrevin [97], cytoplasmic proteins sharing significant homology with the carboxy-terminal domains of dystrophin [98]. The presence of binding domains like PH, SU and PDZ domain allow these scaffold proteins to interact with several other proteins and lipids leading to the building of multi-protein/lipid signalling complexes.
Alpha-Dystrobrevin and its associated proteins in human promyelocytic leukemia cells induced to apoptosis
2012, Journal of ProteomicsCitation Excerpt :It is also possible that src-family kinases phosphorylate DB, since these proteins have been implicated in signal transduction at the maturing neuromuscular junction. Incidentally, some anti-src antibodies cross-reacted with α-DB-1, suggest that they share similar phosphorylated epitopes [7]. Moreover, Senter et al. [8] have shown that dystrophin is a substrate for a variety of protein kinases, such as the CaM kinase, casein kinase II, and protein kinase C, both in vitro and in vivo.
Evolution and comparative genomics of subcellular specializations: EST sequencing of Torpedo electric organ
2011, Marine GenomicsCitation Excerpt :Alternative splicing of α-dystrobrevin (DB) is a valid example of subsynaptic myonuclear domain specialization. DB exists in multiple isoforms including DB1 and DB2 (Balasubramanian et al., 1998; Wagner et al., 1993). DB1, strictly expressed at NMJs and myotendinous junctions (MTJs), has an extended C-terminal domain, which is tyrosine phosphorylated, where as DB2 lacks this domain and is therefore expressed throughout the muscle fiber including NMJ and MTJ.