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contributor authorTang, Dale D.
contributor authorLiao, Guoning
contributor authorGerlach, Brennan D.
date accessioned2019-03-17T09:31:23Z
date available2019-03-17T09:31:23Z
date copyright1/18/2019 12:00:00 AM
date issued2019
identifier issn2572-7958
identifier otherjesmdt_002_01_010801.pdf
identifier urihttp://yetl.yabesh.ir/yetl1/handle/yetl/4255533
description abstractVimentin intermediate filaments (IFs) link to desmosomes (intercellular junctions) on the membrane and dense bodies in the cytoplasm, which provides a structural base for intercellular and intracellular force transmission in smooth muscle. There is evidence to suggest that the vimentin framework plays an important role in mediating smooth muscle mechanical properties such as tension and contractile responses. Contractile activation induces vimentin phosphorylation at Ser-56 and vimentin network reorientation, facilitating contractile force transmission among and within smooth muscle cells. p21-activated kinase 1 and polo-like kinase 1 catalyze vimentin phosphorylation at Ser-56, whereas type 1 protein phosphatase dephosphorylates vimentin at this residue. Vimentin filaments are also involved in other cell functions including migration and nuclear positioning. This review recapitulates our current knowledge how the vimentin network modulates mechanical and biological properties of smooth muscle.
publisherThe American Society of Mechanical Engineers (ASME)
titleReorganization of the Vimentin Network in Smooth Muscle
typeJournal Paper
journal volume2
journal issue1
journal titleJournal of Engineering and Science in Medical Diagnostics and Therapy
identifier doi10.1115/1.4042313
journal fristpage10801
journal lastpage010801-5
treeJournal of Engineering and Science in Medical Diagnostics and Therapy:;2019:;volume( 002 ):;issue: 001
contenttypeFulltext


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