SCS2 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome V.
Dietrich FS, Mulligan J, Hennessy K, Yelton MA, Allen E, Araujo R, Aviles E, Berno A, Brennan T, Carpenter J, Chen E, Cherry JM, Chung E, Duncan M, Guzman E, Hartzell G, Hunicke-Smith S, Hyman RW, Kayser A, Komp C, Lashkari D, Lew H, Lin D, Mosedale D, Davis RW
Nature387(6632 Suppl)78-81(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Data suggest that a specific pool of phosphatidic acid, associated with lipid droplet formation in perinuclear ER, is responsible for initial rapid exit of Opi1p from nucleus to ER and is required for Ino1 expression in presence of choline; interaction between Opi1p and Scs2p in ER membrane facilitates transit of phosphatidic acid from ER to mitochondria.
Title: Interaction between repressor Opi1p and ER membrane protein Scs2p facilitates transit of phosphatidic acid from the ER to mitochondria and is essential for

The deletion of SCS2 did not affect Ca2+ influx activity when calcineurin was inhibited by FK506, but enhanced this activity by 35% when the enzyme was not inhibited. However, this enhancement was canceled by the deletion of ECM7. These results suggest that Cch1/Mid1 is regulated differentially by Ecm7 and Scs2 in a manner that is dependent on the phosphorylation status of Cch1.
Title: Genetic analysis of the regulation of the voltage-gated calcium channel homolog Cch1 by the ? subunit homolog Ecm7 and cortical ER protein Scs2 in yeast.

this study examined the effects of Scs2p levels on the association of Opi1p with the nuclear membrane by both morphologically and biochemically.
Title: Induction of intranuclear membranes by overproduction of Opi1p and Scs2p, regulators for yeast phospholipid biosynthesis, suggests a mechanism for Opi1p nuclear translocation.

Study shows that a direct interaction between the endoplasmic reticulum (ER) protein Scs2 and the septin Shs1 creates the diffusion barrier in yeast. Barrier formation requires Epo1, a novel ER-associated subunit of the polarisome that interacts with Scs2 and Shs1, encoded by the ORF YMR124W.
Title: Polarization of the endoplasmic reticulum by ER-septin tethering.

model predicts that this process involves an acceptor membrane complex containing the C2 domains of Psd2p, PstB2p, and Pbi1p that ligate to Scs2p and phosphatidic acid present in the donor membrane
Title: An assembly of proteins and lipid domains regulates transport of phosphatidylserine to phosphatidylserine decarboxylase 2 in Saccharomyces cerevisiae.