Linked Life Data

10736562

Source:http://linkedlifedata.com/resource/pubmed/id/10736562

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-2-2
pubmed:abstractText
MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Its conformation in solution appears to be labile, with little evidence for definite secondary structure. MARCKS (and MRP) interact inter alia with lipid bilayer membranes (via the myristoyl group and the ED), with protein kinases (which phosphorylate the serines in the ED), and with calmodulin (via the ED); synergies between these diverse interactions present an unusually rich array of possibilities for a variety of regulatory rôles. The proteins appear to be essential for controlling cell shape changes, possibly via involvement in cytoskeleton-membrane linkage. MRP deficiency leads to neural tube defects in brain development; MARCKS overexpression strongly depresses the proliferation of cancer cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1357-2725
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
475-9
pubmed:dateRevised
2005-11-23
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
MARCKS: a case of molecular exaptation?
pubmed:affiliation
Department of Biophysical Chemistry, Biozentrum, 4056, Basel, Switzerland. J.ramsden@unibas.ch
pubmed:publicationType
Journal Article, Review