The lipid-binding SEC14 domain.
Protein-lipid interactions are important for protein targeting, signal transduction, lipid transport, lipid biosynthesis, lipid metabolism, and the maintenance of cellular compartments and membranes. Specific lipid-binding protein domains, such as PH, FYVE, PX, PHD, C2 and SEC14 homology domains, mediate interactions between proteins and specific phospholipids. Here we review the published literature, plus some of our most recent unpublished findings, regarding the biology of the SEC14 domain, also known as CRAL_TRIO domain.
Saito
Kan
K
The Burnham Institute for Medical Research, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Tautz
Lutz
L
Mustelin
Tomas
T
D020816:Amino Acid Motifs; D000818:Animals; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism*; D008958:Models, Molecular; D010716:Phosphatidylinositols / Q000378:metabolism; D049294:Phospholipid Transfer Proteins / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D051381:Rats; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D008563:Membrane Lipids; D010716:Phosphatidylinositols; D049294:Phospholipid Transfer Proteins; C483438:SEC14 protein, S cerevisiae; C100642:SEC14L1 protein, human; D029701:Saccharomyces cerevisiae Proteins; C506000:Sec14p-like phosphoinositide-binding p45 protein, rat