Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6455
pubmed:dateCreated
1994-1-10
pubmed:abstractText
Elucidation of the reactions responsible for the calcium-regulated fusion of secretory granules with the plasma membrane in secretory cells would be facilitated by the identification of participant proteins having known biochemical activities. The successful characterization of cytosolic and vesicle proteins that may function in calcium-regulated secretion has not yet revealed the molecular events underlying this process. Regulated secretion consists of sequential priming and triggering steps which depend on ATP and Ca2+, respectively, and require distinct cytosolic proteins. Characterization of priming-specific factors (PEP proteins) should enable the ATP-requiring reactions to be identified. Here we show that one of the mammalian priming factors (PEP3) is identical to phosphatidylinositol transfer protein (PITP). The physiological role of PITP was previously unknown. We also find that SEC14p, the yeast phosphatidylinositol transfer protein which is essential for constitutive secretion, can substitute for PEP3/PITP in priming. Our results indicate that a role for phospholipid transfer proteins is conserved in the constitutive and regulated secretory pathways.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Norepinephrine, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Transfer Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SEC24 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
366
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
572-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8255295-Adenosine Triphosphate, pubmed-meshheading:8255295-Amino Acid Sequence, pubmed-meshheading:8255295-Animals, pubmed-meshheading:8255295-Brain, pubmed-meshheading:8255295-Calcium, pubmed-meshheading:8255295-Carrier Proteins, pubmed-meshheading:8255295-Cell Membrane Permeability, pubmed-meshheading:8255295-Chromatography, Gel, pubmed-meshheading:8255295-Cytosol, pubmed-meshheading:8255295-Egtazic Acid, pubmed-meshheading:8255295-Kinetics, pubmed-meshheading:8255295-Liver, pubmed-meshheading:8255295-Macromolecular Substances, pubmed-meshheading:8255295-Membrane Proteins, pubmed-meshheading:8255295-Microsomes, pubmed-meshheading:8255295-Molecular Sequence Data, pubmed-meshheading:8255295-Norepinephrine, pubmed-meshheading:8255295-PC12 Cells, pubmed-meshheading:8255295-Phosphatidylinositols, pubmed-meshheading:8255295-Phospholipid Transfer Proteins, pubmed-meshheading:8255295-Rats, pubmed-meshheading:8255295-Saccharomyces cerevisiae Proteins
pubmed:year
1993
pubmed:articleTitle
Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion.
pubmed:affiliation
Program in Cell and Molecular Biology, University of Wisconsin, Madison 53706.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.