Open AccessGenetic and biochemical interactions between the Arp2/3 complex, Cmd1p, casein kinase II, and Tub4p in yeast
Author(s) -
SchaererBrodbeck Claudia,
Riezman Howard
Publication year - 2003
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1016/s1567-1356(03)00110-7
Subject(s) - biology , casein kinase 2 , microbiology and biotechnology , microtubule , tubulin , protein subunit , cytosol , cytoskeleton , actin , mutant , kinase , function (biology) , gene , protein kinase a , biochemistry , cell , mitogen activated protein kinase kinase , enzyme
Arc35p, a component of the Arp2/3 complex, plays at least two distinct roles, regulating the actin cytoskeleton, but also microtubule function during cell division. Both functions involve calmodulin ( CMD1 ). To investigate the pathway affecting microtubule function, we identified genes that are able to suppress the temperature‐sensitive growth defect of the arc35‐1 strain. Genes encoding γ‐tubulin ( TUB4 ) or any subunit of casein kinase II (CKII) suppressed this growth defect, but did not suppress the growth defect of a mutant in another subunit of the Arp2/3 complex, arp2‐1 . We could also show a physical association of Arc35p with subunits of CKII, Cmd1p, and Tub4p. Based on the exclusive localization of Arc35p to the cytosolic Arp2/3 complex and on mutant phenotypes, we propose that the role of the Arc35p/CKII interaction might be to activate a cytosolic pool of γ‐tubulin, likely via calmodulin, for its nuclear and/or cytoplasmic functions.