BSC 300 Lecture Notes - Lecture 16: Immunoglobulin Superfamily, Spina Bifida, Cell Adhesion

• School: University of Alabama
• Department: Biological Sciences
• Course: BSC 300
• Professor: Yoder

Document Summary

Can signal both from extracellular to cytoplasm and from cell to ecm. An inactive integrin dimer sits at the cell surface in a bent conformation incapable o interacting with ecm proteins. Inside out signaling: activation of a number of cytoplasmic ligands binds the cytoplasmic tails and separates the and chains. This induces a conformational change that allows integrin to bind ecm ligands. Such regulation promotes strong interactions between cells and the ecm. Integrin proteins also participate in outside in signaling: extracellular ecm ligands (collagen and fibronectin, primarily) can bind sites in some integrin dimers inducing conformational change. This is mediated via integrin signaling: most cancer cells have lost this anchorage dependency and can exist without connection to the ecm. Focal adhesions: docking sites where cells adhere to their substratum and send signals to the cell interior. Cytoplasmic domains of integrins contain binding sites for a variety of cytoplasmic proteins.