Gene Symbol: BUD14
Description: protein phosphatase regulator BUD14
Alias: protein phosphatase regulator BUD14
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Cullen P, Sprague G. The Glc7p-interacting protein Bud14p attenuates polarized growth, pheromone response, and filamentous growth in Saccharomyces cerevisiae. Eukaryot Cell. 2002;1:884-94 pubmed
    ..Cloning and segregation analysis demonstrated that BUD14 was the affected gene...
  2. Knaus M, Cameroni E, Pedruzzi I, Tatchell K, De Virgilio C, Peter M. The Bud14p-Glc7p complex functions as a cortical regulator of dynein in budding yeast. EMBO J. 2005;24:3000-11 pubmed
    ..Taken together, our results suggest that Bud14p functions as a regulatory subunit of the Glc7p type-I phosphatase to stabilize MT interactions specifically at sites of polarized growth. ..
  3. Lenssen E, James N, Pedruzzi I, Dubouloz F, Cameroni E, Bisig R, et al. The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation--via a newly identified Glc7/Bud14 type I protein phosphatase module--and TFIID promoter distribution. Mol Cell Biol. 2005;25:488-98 pubmed
    ..modification status of Msn2, which depends on the type 1 protein phosphatase Glc7 and its newly identified subunit Bud14. Tests of epistasis as well as transcriptional analyses of Bud14-dependent transcription support a model in which ..
  4. Pinsky B, Kotwaliwale C, Tatsutani S, Breed C, Biggins S. Glc7/protein phosphatase 1 regulatory subunits can oppose the Ipl1/aurora protein kinase by redistributing Glc7. Mol Cell Biol. 2006;26:2648-60 pubmed
    ..To identify potential Glc7 and Ipl1 substrates, we isolated ipl1-321 dosage suppressors. Seven genes (SDS22, BUD14, GIP3, GIP4, SOL1, SOL2, and PEX31) encode newly identified ipl1 dosage suppressors, and all 10 suppressors encode ..
  5. Gould C, Chesarone Cataldo M, Alioto S, Salin B, Sagot I, Goode B. Saccharomyces cerevisiae Kelch proteins and Bud14 protein form a stable 520-kDa formin regulatory complex that controls actin cable assembly and cell morphogenesis. J Biol Chem. 2014;289:18290-301 pubmed publisher
    ..Saccharomyces cerevisiae Bud14 is one member of an emerging class of formin regulators that target the FH2 domain to inhibit actin polymerization,..
  6. Eskin J, Rankova A, Johnston A, Alioto S, Goode B. Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo. Mol Biol Cell. 2016;27:828-37 pubmed publisher
    ..A Smy1-like sequence motif was also identified in a different Bnr1 regulator, Bud14, and found to be essential for Bud14 functions in regulating actin cable architecture and function in vivo...
  7. Chesarone M, Gould C, Moseley J, Goode B. Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function. Dev Cell. 2009;16:292-302 pubmed publisher
    ..Here, we identify Bud14 as a high-affinity inhibitor of the yeast formin Bnr1 that rapidly displaces the Bnr1 FH2 domain from growing ..
  8. Neller J, Dünkler A, Rösler R, Johnsson N. A protein complex containing Epo1p anchors the cortical endoplasmic reticulum to the yeast bud tip. J Cell Biol. 2015;208:71-87 pubmed publisher
    ..This analysis therefore identifies Epo1p as a novel and important component of the polarisome that promotes cER tethering at sites of polarized growth. ..
  9. Ni L, Snyder M. A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol Biol Cell. 2001;12:2147-70 pubmed
    ..Genome-wide screens of defined collections of mutants hold significant promise for dissecting many biological processes in yeast. ..

More Information


  1. Chesarone Cataldo M, Guerin C, Yu J, Wedlich Soldner R, Blanchoin L, Goode B. The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper. Dev Cell. 2011;21:217-30 pubmed publisher
    ..Bnr1 to decrease rates of actin filament elongation, which is distinct from the formin displacement activity of Bud14. In vivo analysis of smy1? mutants demonstrates that this "damper" mechanism is critical for ..
  2. Zarrinpar A, Park S, Lim W. Optimization of specificity in a cellular protein interaction network by negative selection. Nature. 2003;426:676-80 pubmed
    ..System-wide negative selection is a subtle but powerful evolutionary mechanism to optimize specificity within an interaction network composed of overlapping recognition elements. ..
  3. Labedzka K, Tian C, Nussbaumer U, Timmermann S, Walther P, Müller J, et al. Sho1p connects the plasma membrane with proteins of the cytokinesis network through multiple isomeric interaction states. J Cell Sci. 2012;125:4103-13 pubmed publisher
    ..Owing to the overlapping binding specificities of its members the HICS complex is best described as ensembles of isomeric interaction states that precisely coordinate the different functions of the interactors during cytokinesis. ..