QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 14, Issue 9, 3834-3847, September 2003

This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: E03-01-0013v1 14/9/3834    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Huang, C.-F. Articles by Lee, F.-J. S. Search for Related Content PubMed PubMed Citation Articles by Huang, C.-F. Articles by Lee, F.-J. S.

Role for Arf3p in Development of Polarity, but Not Endocytosis, in Saccharomyces cerevisiae

Chun-Fang Huang ^*, Ya-Wen Liu ^*, Luh Tung, Chiou-Hong Lin, and Fang-Jen S. Lee 

Institute of Molecular Medicine, School of Medicine, National Taiwan University, and Department of Medical Research, National Taiwan University Hospital, Taipei, Taiwan, Republic of China

Submitted January 17, 2003; Revised May 8, 2003; Accepted May 23, 2003
Monitoring Editor: Howard Riezman

ADP-ribosylation factors (ARFs) are ubiquitous regulators of virtually every step of vesicular membrane traffic. Yeast Arf3p, which is most similar to mammalian ARF6, is not essential for cell viability and not required for endoplasmic reticulum-to-Golgi protein transport. Although mammalian ARF6 has been implicated in the regulation of early endocytic transport, we found that Arf3p was not required for fluid-phase, membrane internalization, or mating-type receptor-mediated endocytosis. Arf3p was partially localized to the cell periphery, but was not detected on endocytic structures. The nucleotide-binding, N-terminal region, and N-terminal myristate of Arf3p are important for its proper localization. C-Terminally green fluorescent protein-tagged Arf3, expressed from the endogenous promoter, exhibited a polarized localization to the cell periphery and buds, in a cell cycle-dependent manner. Arf3-GFP achieved its proper localization during polarity growth through an actin-independent pathway. Both haploid and homologous diploid arf3 mutants exhibit a random budding defect, and the overexpression of the GTP-bound form Arf3p(Q71L) or GDP-binding defective Arf3p(T31N) mutant interfered with budding-site selection. We conclude that the GTPase cycle of Arf3p is likely to be important for the function of Arf3p in polarizing growth of the emerging bud and/or an unidentified vesicular trafficking pathway.

Abbreviations used: ARF, ADP-ribosylation factor; ER, endoplasmic reticulum; PCR, polymerase chain reaction.

Online version of this article contains supplementary data for some figures. Online version is available at www.molbiolcell.org.

^* These authors contributed equally to this work.

Corresponding author. E-mail address: fangjen{at}ha.mc.ntu.edu.tw.

This article has been cited by other articles:

				J. Ikenouchi and M. Umeda FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex PNAS, January 12, 2010; 107(2): 748 - 753. [Abstract] [Full Text] [PDF]

				S. C. Lee, S. N. Schmidtke, L. J. Dangott, and B. D. Shaw Aspergillus nidulans ArfB Plays a Role in Endocytosis and Polarized Growth Eukaryot. Cell, August 1, 2008; 7(8): 1278 - 1288. [Abstract] [Full Text] [PDF]

				P.-C. Tsai, S.-W. Lee, Y.-W. Liu, C.-W. Chu, K.-Y. Chen, J.-C. Ho, and F.-J. S. Lee Afi1p Functions as an Arf3p Polarization-specific Docking Factor for Development of Polarity J. Biol. Chem., June 13, 2008; 283(24): 16915 - 16927. [Abstract] [Full Text] [PDF]

				H. P. Price, M. Stark, and D. F. Smith Trypanosoma brucei ARF1 Plays a Central Role in Endocytosis and Golgi-Lysosome Trafficking Mol. Biol. Cell, March 1, 2007; 18(3): 864 - 873. [Abstract] [Full Text] [PDF]

				Y.-W. Liu, S.-W. Lee, and F.-J. S. Lee Arl1p is involved in transport of the GPI-anchored protein Gas1p from the late Golgi to the plasma membrane J. Cell Sci., September 15, 2006; 119(18): 3845 - 3855. [Abstract] [Full Text] [PDF]

				J. E. Connolly and J. Engebrecht The Arf-GTPase-Activating Protein Gcs1p Is Essential for Sporulation and Regulates the Phospholipase D Spo14p Eukaryot. Cell, January 1, 2006; 5(1): 112 - 124. [Abstract] [Full Text] [PDF]

				Y.-W. Liu, C.-F. Huang, K.-B. Huang, and F.-J. S. Lee Role for Gcs1p in Regulation of Arl1p at Trans-Golgi Compartments Mol. Biol. Cell, September 1, 2005; 16(9): 4024 - 4033. [Abstract] [Full Text] [PDF]

				A. K. Gillingham, A. H. Y. Tong, C. Boone, and S. Munro The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi J. Cell Biol., October 25, 2004; 167(2): 281 - 292. [Abstract] [Full Text] [PDF]

				R. Cox, R. J Mason-Gamer, C. L. Jackson, and N. Segev Phylogenetic Analysis of Sec7-Domain-containing Arf Nucleotide Exchangers Mol. Biol. Cell, April 1, 2004; 15(4): 1487 - 1505. [Abstract] [Full Text] [PDF]