Michael F. Ingram

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ADP-ribosylation factor appears to regulate the budding of both COPI and clathrin-coated transport vesicles from Golgi membranes. An arf1Delta synthetic lethal screen identified SWA3/DRS2, which encodes an integral membrane P-type ATPase and potential aminophospholipid translocase (or flippase). The drs2 null allele is also synthetically lethal with(More)
BACKGROUND In eukaryotic cells, clathrin-coated vesicles transport specific cargo from the plasma membrane and trans-Golgi network to the endosomal system. Removal of the clathrin coat in vitro requires the uncoating ATPase Hsc70 and its DnaJ cofactor auxilin. To date, a requirement for auxilin and Hsc70 in clathrin function in vivo has not been(More)
The small GTP binding protein ARF has been implicated in budding clathrin-coated vesicles (CCVs) from Golgi and endosomal membranes. An arf1 synthetic lethal screen identified DRS2/SWA3 along with a clathrin heavy-chain conditional allele (chc1-5/swa5-1) and SWA2, encoding the yeast auxilin-like protein involved in uncoating CCVs. Drs2p/Swa3p is a P-type(More)
Apolipoprotein (apo) B and the microsomal triglyceride transfer protein are essential for the hepatic assembly and secretion of triglyceride-rich VLDL. To understand how apoB initiates the process of lipoprotein formation, interest has focused on the biogenesis of its amino terminal globular domain (alpha1 domain). When only this domain is expressed in(More)
The initial assembly of apolipoprotein B100 (apoB) into lipoprotein particles occurs cotranslationally. To examine steps required to initiate this process, the intracellular folding and assembly of the amino-terminal 28% of apoB (apoB28) was examined using several criteria including nonreducing gel electrophoresis, sensitivity to dithiothreitol(More)
Apolipoprotein B (apoB) is essential for the hepatic assembly and secretion of triglyceride-rich very low density lipoproteins. Recent studies have revealed that in both hepatic and nonhepatic cells a large percentage of newly synthesized apoB polypeptides engage in transmembrane interactions with the endoplasmic reticulum (ER). These apoB-membrane(More)
It has been proposed that inefficient translocation across the endoplasmic reticulum (ER) membrane gives rise to transmembrane forms of apolipoprotein B-100 (apoB). However, we previously demonstrated that the amino-terminal 50% of apoB (apoB-50) was efficiently translocated across the ER membrane in the nonhepatic cell line COS-1. To determine whether(More)
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