Calpain2 (m-Calpain) cleaves TLN1 (Talin-1)

Stable Identifier
R-HSA-9855106
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Calpain2 cleaves TLN1 (Talin-1) between amino acid residues 433 and 434 (inferred from mouse homologs). Endothelial cells contain Calpain1 (mu-Calpain) and Calpain2 (m-Calpain) (Fujitani et al. 1997, Zhang et al. 2017). Endothelial Calpain2 is activated by calcium in response to laminar shear stress and cleaves TLN1 and VCL (Vinculin) (Miyazaki et al. 2007, 2010) of the cytoskeleton to alter the shape of the endothelial cell such that its long axis becomes parallel with the fluid flow.
Literature References
PubMed ID Title Journal Year
17596297 Requirement of Ca2+ influx- and phosphatidylinositol 3-kinase-mediated m-calpain activity for shear stress-induced endothelial cell polarity

Miyazaki, T, Honda, K, Ohata, H

Am J Physiol Cell Physiol 2007
32848880 Inside Out Integrin Activation Mediated by PIEZO1 Signaling in Erythroblasts

Aglialoro, F, Hofsink, N, Hofman, M, Brandhorst, N, van den Akker, E

Front Physiol 2020
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Catalyst Activity

calcium-dependent cysteine-type endopeptidase activity of Calpain2:Ca2+ [plasma membrane]

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