Lecture Notes 10-31-08 - SH2andSH3Domains

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SH2 and SH3 Domains SH2 domains recognize specific phosphorylated  tyrosines (SH2 binding motifs) SH3 domains bind to proline rich motifs in  intracellular proteins
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Ras There are multiple Ras proteins, which all belong  to a large family of monomeric GTPases Ras helps broadcast signals from the cell  surface to other parts of the cell, acting as a  signaling hub Ras proteins contain a covalently attached lipid  group that anchors the protein in the plasma  membrane Ras is often required when receptor tyrosine  kinases signal to the nucleus to stimulate cell  proliferation or differentiation by changing gene  expression
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Ras functions as a  molecular switch It is active when GTP  is bound and inactive  when GDP is bound Guanine nucleotide  exchange factors  (GEFs) stimulate the  dissociation of GDP  and uptake of GTP GTPase-activating  proteins (GAPs)  increase the  hydrolysis of bound  GTP by Ras It is the regulation of  the activity of GEFs  that controls Ras  function
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In most cases, adapter proteins link  receptor tyrosine kinases to Ras Drk is an adapter protein that binds  through its SH2 domain to specific  phosphotyrosines on activated tyrosine  kinase receptors Drk binds through its SH3 domain to  proline-rich motifs on a GEF called Sos
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This note was uploaded on 02/22/2010 for the course BE 2400 taught by Professor Goldman during the Fall '08 term at Michigan Technological University.

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Lecture Notes 10-31-08 - SH2andSH3Domains

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