Structural highlights
Function
[MYOM1_MOUSE] May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. May also contact myosin filaments. Also binds beta-integrins.
Publication Abstract from PubMed
Over the last two decades, our knowledge concerning intracellular events that regulate integrin's affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development of focal complexes, which could further mature to form focal adhesions, still remains under-investigated. Here we present a structural model of tandem IgC2 domains of skelemin in complex with the cytoplasmic tails of integrin alphaIIbbeta3. The model is generated based upon NMR data and this tertiary assembly illuminates a potential link between the essential cell adhesion receptors and myosin filaments. This connection may serve as a basis for generating the mechanical forces necessary for cell migration and remodeling.
Skelemin Association with AlphaIIbBeta3 Integrin: A Structural Model.,Gorbatyuk V, Nguyen K, Podolnikova NP, Deshmukh L, Lin X, Ugarova TP, Vinogradova O Biochemistry. 2014 Sep 15. PMID:25224262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gorbatyuk V, Nguyen K, Podolnikova NP, Deshmukh L, Lin X, Ugarova TP, Vinogradova O. Skelemin Association with AlphaIIbBeta3 Integrin: A Structural Model. Biochemistry. 2014 Sep 15. PMID:25224262 doi:http://dx.doi.org/10.1021/bi500680s
