Avtor/Urednik		Chao, Steven; Benowitz, Larry I; Krainc, Dimitri; Irwin, Nina
Naslov		Use of a two-hybrid system to investigate molecular interactions of GAP-43
Tip		članek
Vir		Brain Res Mol Brain Res
Vol. in št.		Letnik 40, št. 2
Leto izdaje		1996
Obseg		str. 195-202
Jezik		eng
Abstrakt		We used the 'interaction trap' (two-hybrid system) to identify polypeptides that interact with the neuronal phosphoprotein, GAP-43, in an intracellular environment. GAP-43 (neuromodulin, B-50, F1), a protein kinase C (PKC) substrate important for the growth and plasticity of neuronal connections, has been implicated in vitro in several signal transduction pathways. In the yeast-based cloning system, the only strong interaction that was detected between GAP-43 and the calcium effector protein, calmodulin (CaM). PKC phosphorylates GAP-43 on serine 41. When we changed this serine to an aspartate residue to mimic constitutive phosphorylation, the interaction with CaM was blocked. Surprisingly, the N-terminal third of GAP-43 alone bound CaM more strongly than did intact GAP-43, suggesting that the protein's C-terminus may play a role in modulating the interaction with CaM. These results, along with other recent findings, suggest a novel role for the interaction between GAP-43 and CaM.
Deskriptorji		CALMODULIN CELL MEMBRANE CHROMOSOME MAPPING MEMBRANE GLYCOPROTEINS MUTATION NERVE TISSUE PROTEINS PLASMIDS