TY - JOUR
T1 - The vesicular transport protein Cgp1p/Vps54p/Tcs3p/Luv1p is required for the integrity of the actin cytoskeleton
AU - Fiedler, T. A.
AU - Karpova, T. S.
AU - Fleig, U.
AU - Young, M. E.
AU - Cooper, J. A.
AU - Hegemann, Johannes H.
N1 - Funding Information:
Acknowledgements This work was supported by grants from the FAZIT-Stiftung and EUROFAN (to JHH) and NIH grant GM 47337 (to JAC). Sabine Klein is thanked for FACS analysis and Christopher P. Mill for technical assistance. We thank Peter Novick for plasmids.
PY - 2002
Y1 - 2002
N2 - The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene (CPF1) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δcgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δcgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in vesicular protein transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of vesicular protein transport with the organization of the actin cytoskeleton.
AB - The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene (CPF1) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δcgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δcgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in vesicular protein transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of vesicular protein transport with the organization of the actin cytoskeleton.
KW - Actin cytoskeleton
KW - CPF1
KW - Chromosome segregation
KW - Saccharomyces cerevisiae
KW - Vesicular protein trafficking
UR - http://www.scopus.com/inward/record.url?scp=0036460642&partnerID=8YFLogxK
U2 - 10.1007/s00438-002-0748-4
DO - 10.1007/s00438-002-0748-4
M3 - Article
C2 - 12395193
AN - SCOPUS:0036460642
SN - 1617-4615
VL - 268
SP - 190
EP - 205
JO - Molecular Genetics and Genomics
JF - Molecular Genetics and Genomics
IS - 2
ER -