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  p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix.

Johnsson, N., Marriott, G., & Weber, K. (1988). p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix. EMBO Journal, 7(8), 2435-2442.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-4D07-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-4D09-9
Genre: Journal Article

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Johnsson, N.1, Author              
Marriott, G.2, Author              
Weber, K.1, Author              
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1Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578618              
2Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 Abstract: Protein I is a hetero-tetramer which contains two copies each of p11 and p36. p36 (calpactin I, lipocortin II) is a major substrate of retrovirally encoded tyrosine protein kinases, while p11 modulates several Ca2+-induced properties also displayed by p36 alone. Here we have characterized the p11 binding site on p36 by fluorescence spectroscopy using porcine p36 labelled at cysteine 8 with the fluorophore Prodan (6-proprionyl-2-dimethylamino-naphthalene). We have used peptides of differing length from the amino-terminal domain of p36 to restrict the major binding site to the first 12 residues. Noticeable binding is still observed with a peptide containing only the first nine residues. Interestingly the N-terminal acetyl group of p36 forms a functional part of the p11 binding site. CD studies indicate that the binding region can form an alpha-helix, which seems to have amphiphatic properties when projected on a helical wheel. This structural element is also known for a calmodulin binding protein. Thus the question is raised whether other p11/calmodulin-related proteins interact with their target proteins via a similar mechanism. We also discuss how p11 could modulate p36 associated properties.

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Language(s): eng - English
 Dates: 1988-08
 Publication Status: Published in print
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Title: EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 7 (8) Sequence Number: - Start / End Page: 2435 - 2442 Identifier: -