rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
1998-7-23
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pubmed:abstractText |
In mammalian cells, the formation of DNA strand breaks is accompanied by synthesis of poly(ADP-ribose). This nucleic acid-like homopolymer may modulate protein functions by covalent and/or noncovalent interactions. Here we show that poly(ADP-ribose) binds strongly to the proteins of the myristoylated alanine-rich C kinase substrate (MARCKS) family, MARCKS and MARCKS-related protein (also MacMARCKS or F52). MARCKS proteins are myristoylated proteins associated with membranes and the actin cytoskeleton. As targets for both protein kinase C (PKC) and calmodulin (CaM), MARCKS proteins are thought to mediate cross-talk between these two signal transduction pathways. Dot blot assays show that poly(ADP-ribose) binds to MARCKS proteins at the highly basic effector domain. Complex formation between MARCKS-related protein and CaM as well as phosphorylation of MARCKS-related protein by the catalytic subunit of PKC are strongly inhibited by equimolar amounts of poly(ADP-ribose), suggesting a high affinity of poly(ADP-ribose) for MARCKS-related protein. Binding of MARCKS-related protein to membranes is also inhibited by poly(ADP-ribose). Finally, poly(ADP-ribose) efficiently reverses the actin-filament bundling activity of a peptide corresponding to the effector domain and inhibits the formation of actin filaments in vitro. Our results suggest that MARCKS proteins and actin could be targets of the poly(ADP-ribose) DNA damage signal pathway.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Poly Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/myristoylated alanine-rich C...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9520-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9649335-Actins,
pubmed-meshheading:9649335-Amino Acid Sequence,
pubmed-meshheading:9649335-Animals,
pubmed-meshheading:9649335-Calmodulin,
pubmed-meshheading:9649335-Humans,
pubmed-meshheading:9649335-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9649335-Membrane Lipids,
pubmed-meshheading:9649335-Membrane Proteins,
pubmed-meshheading:9649335-Mice,
pubmed-meshheading:9649335-Molecular Sequence Data,
pubmed-meshheading:9649335-Phosphorylation,
pubmed-meshheading:9649335-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:9649335-Poly Adenosine Diphosphate Ribose,
pubmed-meshheading:9649335-Polymers,
pubmed-meshheading:9649335-Protein Binding,
pubmed-meshheading:9649335-Protein Kinase C,
pubmed-meshheading:9649335-Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Poly(ADP-ribose) modulates the properties of MARCKS proteins.
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pubmed:affiliation |
Department of Biophysical Chemistry, Biozentrum, University of Basel, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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