@article {1355,
	title = {Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane},
	journal = {Traffic},
	volume = {7},
	number = {11},
	year = {2006},
	note = {ISI Document Delivery No.: 093GOTimes Cited: 30Cited Reference Count: 76Chen, Sophie Wang, Jiyi Muthusamy, Baby-Periyanayaki Liu, Ke Zare, Sara Andersen, Raymond J. Graham, Todd R.},
	month = {Nov},
	pages = {1503-1517},
	type = {Article},
	abstract = {Drs2p, a P-type adenosine triphosphatase required for a phosphatidylserine (PS) flippase activity in the yeast trans Golgi network (TGN), was first implicated in protein trafficking by a screen for mutations synthetically lethal with arf1 (swa). Here, we show that SWA4 is allelic to CDC50, encoding a membrane protein previously shown to chaperone Drs2p from the endoplasmic reticulum to the Golgi complex. We find that cdc50 Delta exhibits the same clathrin-deficient phenotypes as drs2 Delta, including delayed transport of carboxypeptidase Y to the vacuole, mislocalization of resident TGN enzymes and the accumulation of aberrant membrane structures. These trafficking defects precede appearance of cell polarity defects in cdc50 Delta, suggesting that the latter are a secondary consequence of disrupting Golgi function. Involvement of Drs2p-Cdc50p in PS translocation suggests a role in restricting PS to the cytosolic leaflet of the Golgi and plasma membrane. Annexin V binding and papuamide B hypersensitivity indicate that drs2 Delta or cdc50 Delta causes a loss of plasma membrane PS asymmetry. However, clathrin and other endocytosis null mutants also exhibit a comparable loss of PS asymmetry, and studies with drs2-ts and clathrin (chc1-ts) conditional mutants suggest that loss of plasma membrane asymmetry is a secondary consequence of disrupting protein trafficking.},
	keywords = {annexin V, ATPase, B, CARBOXYPEPTIDASE-Y, Cdc50p, clathrin, CLATHRIN-COATED VESICLES, Drs2p, flippase, Golgi complex, GOLGI-COMPLEX, IN-VIVO, INTRAHEPATIC CHOLESTASIS, P-type, P-TYPE ATPASES, papuamide, phosphatidylserine, PHOSPHOLIPID, PUTATIVE AMINOPHOSPHOLIPID, SACCHAROMYCES-CEREVISIAE, TRANSLOCASES, TRANSLOCATION, VACUOLAR PROTEINS},
	isbn = {1398-9219},
	url = {<Go to ISI>://000241156500008},
	author = {Chen, S. and Wang, J. Y. and Muthusamy, B. P. and Liu, K. and Zare, S. and Andersen, R. J. and Graham, T. R.}
}
@article {5220,
	title = {Glanvillic acids A and B and methyl capucinoate A, new metabolites isolated from the Caribbean sponges Plakortis halichondrioides and Plakinastrella onkodes},
	journal = {Journal of Natural Products},
	volume = {64},
	number = {3},
	year = {2001},
	note = {ISI Document Delivery No.: 415MPTimes Cited: 9Cited Reference Count: 17},
	month = {Mar},
	pages = {281-285},
	type = {Article},
	abstract = {Glanvillic acids A (2) and B (3) and the cytotoxic cyclic peroxides methyl capucinoate A (4) and 5 were isolated from the Dominican marine sponges Plakortis halichondrioides and Plakinastrella onkodes, respectively. The structures have been elucidated by spectroscopic analysis of 4 and 5 and of methyl glanvillates A (6) and B (7).},
	keywords = {ACTIVATORS, ANGULOSPICULATUS, ATPase, CYCLIC PEROXIDES},
	isbn = {0163-3864},
	url = {<Go to ISI>://000167725600001},
	author = {Williams, D. E. and Allen, T. M. and Van Soest, R. and Behrisch, H. W. and Andersen, R. J.}
}
