Functional Characterization of ADP-Ribosylation Factor-Like Protein 1 in Saccharomyces cerevisiae
Date Issued
2006
Date
2006
Author(s)
Liu, Ya-Wen
DOI
en-US
Abstract
ADP-ribosylation factors (ARFs) are highly conserved small GTP-binding proteins that enhance the ADP-ribosyltransferase activity of cholera toxin and have an important role in vesicular transport. Several ARF-like proteins (ARLs) have been cloned from different organisms but the biological functions of ARLs remain largely unknown. In this dissertation, an ARL protein, Arl1p, of yeast Saccharomyces cerevisiae was characterized. Yeast ARL1 encodes a protein that is structurally related to human, rat, and Drosophila ARL1 proteins. Here we identified two interacting proteins of Arl1p, Imh1p and Gcs1p, the former is a tethering factor and the latter is an ARFGAP. From several in vitro and in vivo analysis, we demonstrated that Imh1p is a downstream effector of Arl1p and is recruited by the proper protein-protein interaction; on the other hand, Gcs1p exhibits GAP activity toward Arl1p and is able to regulate subcellular localization of Arl1p thus indicates that Gcs1p is a GAP for Arl1p. To the functional analysis, we found that Arl1p is involved in the anterograde transport from the Golgi to cell surface of the glycosylphosphatidylinositol (GPI)-anchored plasma membrane-resident protein Gas1p, but not those cell wall-localized GPI-anchored proteins Crh1p, Crh2p, and Cwp1p, or non-GPI-anchored plasma membrane-protein Gap1p. We also show that regulators of Arl1p: Sys1p, Arl3p, and Gcs1p; and effector Imh1p, all participate in the transport of Gas1p. From these results, not only the first ARL GAP is identified, but the first endogenous cargo molecule of yeast Arl1p is defined.
Subjects
腺嘌呤核苷
二磷酸核醣化因子 囊泡運輸
ARF vesicular trafficking
SDGs
Type
other
File(s)![Thumbnail Image]()
Loading...
Name
ntu-95-F89448006-1.pdf
Size
23.31 KB
Format
Adobe PDF
Checksum
(MD5):7b43d58da3327291db6d6cb3357f6e87