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https://www.readbyqxmd.com/read/23690969/fermitins-the-orthologs-of-mammalian-kindlins-regulate-the-development-of-a-functional-cardiac-syncytium-in-drosophila-melanogaster
#1
James H Catterson, Margarete M S Heck, Paul S Hartley
The vertebrate Kindlins are an evolutionarily conserved family of proteins critical for integrin signalling and cell adhesion. Kindlin-2 (KIND2) is associated with intercalated discs in mice, suggesting a role in cardiac syncytium development; however, deficiency of Kind2 leads to embryonic lethality. Morpholino knock-down of Kind2 in zebrafish has a pleiotropic effect on development that includes the heart. It therefore remains unclear whether cardiomyocyte Kind2 expression is required for cardiomyocyte junction formation and the development of normal cardiac function...
2013: PloS One
https://www.readbyqxmd.com/read/21385318/interaction-between-very-kind-ras-guanine-exchange-factor-and-microtubule-associated-protein-2-and-its-role-in-dendrite-growth-structure-and-function-of-the-second-kinase-noncatalytic-c-lobe-domain
#2
Jinhong Huang, Asako Furuya, Kanehiro Hayashi, Teiichi Furuichi
The kinase noncatalytic C-lobe domain (KIND) is a putative protein-protein interaction module. Four KIND-containing proteins, Spir-2 (actin-nuclear factor), PTPN13 (protein tyrosine phosphatase), FRMPD2 (scaffold protein) and very-KIND (v-KIND) (brain-specific Ras guanine nucleotide exchange factor), have been identified to date. Uniquely, v-KIND has two KINDs (i.e. KIND1 and KIND2), whereas the other three proteins have only one. The functional role of KIND, however, remains unclear. We previously demonstrated that v-KIND interacts with the high-molecular weight microtubule-associated protein 2 (MAP2), a dendritic microtubule-associated protein, leading to negative regulation of neuronal dendrite growth...
May 2011: FEBS Journal
https://www.readbyqxmd.com/read/19854292/the-role-of-kindlins-in-cell-biology-and-relevance-to-human-disease
#3
REVIEW
J E Lai-Cheong, M Parsons, J A McGrath
The kindlins represent a class of focal adhesion proteins implicated in integrin activation. They comprise three evolutionarily conserved members, kindlin-1, kindlin-2 and kindlin-3, that share considerable sequence and structural similarities. The kindlins have a bipartite FERM (four point one protein, ezrin, radixin, moesin) domain interrupted by a pleckstrin homology domain and can bind directly to various classes of integrins as well as participate in inside-out integrin activation. They are encoded by three different genes, namely KIND1 (FERMT1; chromosome 20p12...
May 2010: International Journal of Biochemistry & Cell Biology
https://www.readbyqxmd.com/read/18528435/colocalization-of-kindlin-1-kindlin-2-and-migfilin-at-keratinocyte-focal-adhesion-and-relevance-to-the-pathophysiology-of-kindler-syndrome
#4
J E Lai-Cheong, S Ussar, K Arita, I R Hart, J A McGrath
Kindler syndrome (KS) results from pathogenic loss-of-function mutations in the KIND1 gene, which encodes kindlin-1, a focal adhesion and actin cytoskeleton-related protein. How and why abnormalities in kindlin-1 disrupt keratinocyte cell biology in KS, however, is not yet known. In this study, we identified two previously unreported binding proteins of kindlin-1: kindlin-2 and migfilin. Co-immunoprecipitation and confocal microscopy studies show that these three proteins bind to each other and colocalize at focal adhesion in HaCaT cells and normal human keratinocytes...
September 2008: Journal of Investigative Dermatology
https://www.readbyqxmd.com/read/17984326/very-kind-a-kind-domain-containing-rasgef-controls-dendrite-growth-by-linking-ras-small-gtpases-and-map2
#5
Jinhong Huang, Asako Furuya, Teiichi Furuichi
The regulation of cytoskeletal components in the dendritic shaft core is critical for dendrite elongation and branching. Here, we report that a brain-specific Ras guanine nucleotide exchange factor (RasGEF) carrying two kinase non-catalytic C-lobe domains (KINDs), very-KIND (v-KIND), regulates microtubule-associated protein 2 (MAP2). v-KIND is expressed in developing mouse brain, predominantly in the cerebellar granule cells. v-KIND not only activates Ras small GTPases via the C-terminal RasGEF domain, but also specifically binds to MAP2 via the second KIND domain (KIND2), leading to threonine phosphorylation of MAP2...
November 5, 2007: Journal of Cell Biology
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