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553509
Allosteric Regulation by Protein Phosphorylation
Descrição
Undergraduate Cellular Pathology Mapa Mental sobre Allosteric Regulation by Protein Phosphorylation, criado por Sophie Barrett em 16-02-2014.
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cellular pathology
cellular pathology
undergraduate
Mapa Mental por
Sophie Barrett
, atualizado more than 1 year ago
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Criado por
Sophie Barrett
quase 11 anos atrás
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Resumo de Recurso
Allosteric Regulation by Protein Phosphorylation
Major mechanism by which cells response to extracelluar stimuli
e.g. hormones, light, neutrophic factors, cytokines
Virtually every kind of neuronal protein is regulated by phosphorylation
Protein Kinase transfers phosphate groups from ATP to side chains of serine, threonine or tyrosine on the substrate protein.
How is the activity of the substrate protein terminated?
By protein phosphatase = dephosphorylates by hydrolysis
Protein Kinases may also activate or modify other protein kinases downstream, or transcription factors such as ERK
There are 2 kinds of Protein Kinases
99% phosphorylate serine or threonine residues
e.g. cAMP-dependant PKA which when activated translocates to nucleus to phosphorylate CREB on residue ser133.
1% phosphorylate tyrosine kinases (PTK)
e.g. growth-factor receptors where ligand binding induces dimerisation and the Tyr residues are transphosphorylated
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