Molecular Playground/IntegrinBeta1: Difference between revisions
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==Function== | ==Function== | ||
Integrins are a class of surface proteins that bind to extracellular matrix components and transmit chemical and mechanical cues to internal signaling pathways. Integrin beta 1 binds many proteins when dimerized with an alpha subunit, including collagen, laminin and fibronectin. | Integrins are a class of surface proteins that bind to extracellular matrix components and transmit chemical and mechanical cues to internal signaling pathways. Integrin beta 1 binds many proteins when dimerized with an alpha subunit, including collagen, laminin and fibronectin. Integrin adhesion to the extra cellular matrix is key for cell ability to adhere, migrate and proliferate in both 2D and 3D systems. These will eventually form adhesion complexes, which regulate actomyocin polymerization. During migration, cells continually form new focal adhesions at the leading edge of the cell and release adhesion complexes at the back of the cell, enabling forward movement. | ||
Here are the <scene name='60/609772/N-acetyl-d-glucosamine/2'>N-acetyl-d-glucosamine locations!</scene> N-acetyl-D-glucosamine may regulate integrin signaling during cancer cell migration.[1] | |||
==Integrins and cancer== | ==Integrins and cancer== | ||
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==References== | ==References== | ||
[1] C. Saravanan, F. Liu, I.K. Gipson and N. Panjwani1. Galectin-3 promotes lamellipodia formation in epithelial cells by interacting with complex N-glycans on 31 integrin. Journal of Cell Science 122, 3684-3693 Published by The Company of Biologists (2009). doi:10.1242/jcs.045674. | |||
