Linked Life Data

16470652

Source:http://linkedlifedata.com/resource/pubmed/id/16470652

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2006-3-13
pubmed:abstractText
Intracellular Ca2+ signals are transduced by the binding of Ca2+ to sensor proteins, which subsequently modify the activity of their target proteins. Identification of these target proteins is, therefore, important for an understanding of cellular signalling processes. We have investigated the binding partners of four EF-hand Ca2+-binding proteins. Three proteins of the neuronal calcium sensor (NCS) family, hippocalcin, NCS-1 and neurocalcin delta were prepared as N-terminally tagged GST fusion proteins, and the less closely related protein L-CaBP1 was prepared in both N- and C-terminally tagged forms, the latter requiring generation of a new vector. Immobilised fusion proteins were used to purify binding partners from bovine brain cytosol and membrane extracts in the presence of 1 microM free Ca2+. Bound proteins were eluted with Ca2+-free and high-salt buffers and eluted proteins were identified by MALDI-MS and Western blotting. New protein targets detected included ARF1, Ca2+-dependent activator protein for secretion 1, cyclic nucleotide 3',5'-phosphodiesterase, the vacuolar ATPase, AP1 and AP2 complexes and the type I TGF-beta receptor. While certain of these interactions occurred with more than one of the Ca2+-binding proteins, others were found to be specific targets for particular Ca2+ sensors, and many of these did not overlap with known calmodulin-binding proteins. These findings provide new clues to the functional roles of the neuronal calcium sensor proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1615-9853
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1822-32
pubmed:dateRevised
2007-8-13
pubmed:meshHeading
pubmed-meshheading:16470652-Animals, pubmed-meshheading:16470652-Blotting, Western, pubmed-meshheading:16470652-Brain Chemistry, pubmed-meshheading:16470652-Calcium-Binding Proteins, pubmed-meshheading:16470652-Cattle, pubmed-meshheading:16470652-Cytosol, pubmed-meshheading:16470652-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16470652-Escherichia coli, pubmed-meshheading:16470652-Glutathione Transferase, pubmed-meshheading:16470652-Hippocalcin, pubmed-meshheading:16470652-Mass Spectrometry, pubmed-meshheading:16470652-Membrane Proteins, pubmed-meshheading:16470652-Neurocalcin, pubmed-meshheading:16470652-Receptors, Transforming Growth Factor beta, pubmed-meshheading:16470652-Recombinant Fusion Proteins, pubmed-meshheading:16470652-Reproducibility of Results, pubmed-meshheading:16470652-Spectrometry, Mass, Matrix-Assisted Laser...
pubmed:year
2006
pubmed:articleTitle
Analysis of the interacting partners of the neuronal calcium-binding proteins L-CaBP1, hippocalcin, NCS-1 and neurocalcin delta.
pubmed:affiliation
The Physiological Laboratory, School of Biomedical Sciences, University of Liverpool, Liverpool, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't