| pubmed-article:9649335 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9649335 | lifeskim:mentions | umls-concept:C0032403 | lld:lifeskim |
| pubmed-article:9649335 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:9649335 | lifeskim:mentions | umls-concept:C0067072 | lld:lifeskim |
| pubmed-article:9649335 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:9649335 | pubmed:dateCreated | 1998-7-23 | lld:pubmed |
| pubmed-article:9649335 | 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. | lld:pubmed |
| pubmed-article:9649335 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9649335 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9649335 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9649335 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9649335 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:9649335 | pubmed:author | pubmed-author:AlthausF RFR | lld:pubmed |
| pubmed-article:9649335 | pubmed:author | pubmed-author:VergèresGG | lld:pubmed |
| pubmed-article:9649335 | pubmed:author | pubmed-author:KleczkowskaH... | lld:pubmed |
| pubmed-article:9649335 | pubmed:author | pubmed-author:SchmittA KAK | lld:pubmed |
| pubmed-article:9649335 | pubmed:author | pubmed-author:PleschkeJ MJM | lld:pubmed |
| pubmed-article:9649335 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9649335 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:9649335 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:9649335 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9649335 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9649335 | pubmed:pagination | 9520-7 | lld:pubmed |
| pubmed-article:9649335 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:9649335 | pubmed:meshHeading | pubmed-meshheading:9649335-... | lld:pubmed |
| pubmed-article:9649335 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9649335 | pubmed:articleTitle | Poly(ADP-ribose) modulates the properties of MARCKS proteins. | lld:pubmed |
| pubmed-article:9649335 | pubmed:affiliation | Department of Biophysical Chemistry, Biozentrum, University of Basel, Switzerland. | lld:pubmed |
| pubmed-article:9649335 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9649335 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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