Linked Life Data

16118014

Source:http://linkedlifedata.com/resource/pubmed/id/16118014

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-12-6
pubmed:abstractText
PITPs regulate the interface between lipid metabolism and cellular functions, but the fundamental nature of this regulation is not understood. Yeast and mouse studies demonstrate strict coupling of individual PITPs to specific cellular activities, but the invisibility of these specificities in in vitro models for PITP activity is remarkable. In our opinion, delineation of PITP functions requires the continued application of genetic approaches such as those summarized here. Future studies dedicated to enhancing our understanding of the mechanisms of action of Sec14p-like and metazoan PITPs are worthy goals for three reasons. First, it is becoming abundantly clear that PITPs act at important biological interfaces that involve lipid and protein trafficking, phospholipid biosynthesis and polarized membrane growth. Because these interfaces are critical not only to cellular functions, but also to developmental processes, the function of PITPs in development of multicellular organisms is a particularly attractive area of research that remains essentially untapped. Second, the yeast studies indicate functional linkages between Sec14p-like PITPs and members of ubiquitous but entirely uncharacterized eukaryotic proteins such as OSBP family members. Finally, the link of PITPs to disease is already clear since PITP deficiencies lie at the foundation of novel mechanisms of neurodegenerative, glucose homeostatic and gastrointestinal disorders in mammals. Given that the contribution of Sec14p-like proteins to the PITP complement of mammalian cells is completely uninvestigated, and that the mammalian genome encodes many proteins of this class, we anticipate such advances will directly and positively impact our understanding of the molecular basis of such diseases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2571
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-70
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae.
pubmed:affiliation
Department of Cell and Developmental Biology, University of North Carolina School of Medicine, Chapel Hill, NC 27599-7090, USA. vytas@med.unc.edu
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural