|
|
|
|
A more recent version of this article appeared on October 1, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on May 7, 2002
Revised on June 26, 2002
Accepted on July 8, 2002
1 The Henry Wellcome Laboratory for Cell Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, UK
2 Wellcome Trust Biocentre, Division of Molecular Cell Biology, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH
* Corresponding author. E-mail address: k.ayscough{at}bio.gla.ac.uk.
The importance of coupling the process of endocytosis to factors regulating actin dynamics has been clearly demonstrated in yeast, and many proteins involved in these mechanisms have been identified and characterised. Here we demonstrate the importance of two additional cortical components, Ysc84p and Lsb5p, which together are essential for the organisation of the actin cytoskeleton and for fluid phase endocytosis. Both Ysc84p and Lsb5p were identified through two hybrid screens with different domains of the adaptor protein Sla1p. Ysc84p co-localises with cortical actin and requires the presence of an intact actin cytoskeleton for its cortical localisation. Ycl034w/Lsb5p localises to the cell cortex but does not co-localise with actin. The Lsb5 protein contains putative VHS and GAT domains as well as an NPF motif which are all domains characteristic of proteins involved in membrane trafficking. Deletion of either gene alone does not confer any dramatic phenotype on cells. However, deletion of both genes is lethal at elevated temperatures. Furthermore, at all temperatures this double mutant has depolarised actin and an almost undetectable level of fluid phase endocytosis. Our data demonstrates that Ysc84p and Lsb5p are important components of complexes involved in overlapping pathways coupling endocytosis with the actin cytoskeleton in yeast.
This article has been cited by other articles:
![]() |
O. Quintero-Monzon, A. A. Rodal, B. Strokopytov, S. C. Almo, and B. L. Goode Structural and Functional Dissection of the Abp1 ADFH Actin-binding Domain Reveals Versatile In Vivo Adapter Functions Mol. Biol. Cell, July 1, 2005; 16(7): 3128 - 3139. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Monzo, N. C. Gauthier, F. Keslair, A. Loubat, C. M. Field, Y. Le Marchand-Brustel, and M. Cormont Clues to CD2-associated Protein Involvement in Cytokinesis Mol. Biol. Cell, June 1, 2005; 16(6): 2891 - 2902. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. K. Mattila, O. Quintero-Monzon, J. Kugler, J. B. Moseley, S. C. Almo, P. Lappalainen, and B. L. Goode A High-affinity Interaction with ADP-Actin Monomers Underlies the Mechanism and In Vivo Function of Srv2/cyclase-associated Protein Mol. Biol. Cell, November 1, 2004; 15(11): 5158 - 5171. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. H. Cox, J. J. Tate, and T. G. Cooper Actin Cytoskeleton Is Required For Nuclear Accumulation of Gln3 in Response to Nitrogen Limitation but Not Rapamycin Treatment in Saccharomyces cerevisiae J. Biol. Chem., April 30, 2004; 279(18): 19294 - 19301. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. W. Gourlay, H. Dewar, D. T. Warren, R. Costa, N. Satish, and K. R. Ayscough An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast J. Cell Sci., June 15, 2003; 116(12): 2551 - 2564. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Suer, S. Misra, L. F. Saidi, and J. H. Hurley Structure of the GAT domain of human GGA1: A syntaxin amino-terminal domain fold in an endosomal trafficking adaptor PNAS, April 15, 2003; 100(8): 4451 - 4456. [Abstract] [Full Text] [PDF] |
||||