K
Kathleen L. Gould
Researcher at Vanderbilt University
Publications - 233
Citations - 15753
Kathleen L. Gould is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Schizosaccharomyces pombe & Cytokinesis. The author has an hindex of 69, co-authored 206 publications receiving 15016 citations. Previous affiliations of Kathleen L. Gould include University of California, San Diego & University of Washington.
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Journal ArticleDOI
Dephosphorylation of F-BAR Protein Cdc15 Modulates Its Conformation and Stimulates Its Scaffolding Activity at the Cell Division Site
Rachel H. Roberts-Galbraith,Melanie D. Ohi,Bryan A. Ballif,Jun-Song Chen,Ian McLeod,W. Hayes McDonald,Steven P. Gygi,John R. Yates,Kathleen L. Gould +8 more
TL;DR: The results indicate that Cdc15 phosphoregulation impels both assembly and disassembly of the contractile apparatus and suggest a regulatory strategy that PCH family and BAR superfamily members might broadly employ to achieve temporal specificity in their roles as linkers between membrane and cytoskeleton.
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The Schizosaccharomyces Pombe Actin-Related Protein, Arp3, Is a Component of the Cortical Actin Cytoskeleton and Interacts With Profilin
TL;DR: Key findings are presented that define an essential role for Arp3p in the functioning of the cortical actin cytoskeleton and believe that this complex may mediate the cortical functions of profilin at actin patches in S. pombe.
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Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing.
W. Hayes McDonald,Ryoma Ohi,Natalia V. Smelkova,David Frendewey,Kathleen L. Gould,Kathleen L. Gould +5 more
TL;DR: It is shown that cDC5p associates with the U2, U5, and U6 snRNAs and that cells lackingcdc5 + function are defective in pre-mRNA splicing, raising the possibility that the cdc5p complex is an intermediate in the assembly or disassembly of an active S. pombe spliceosome.
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Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast.
TL;DR: It is shown by biochemical and mutational studies that the S.pombe actomyosin ring component Cdc4p is a light chain associated with Myo2p, a myosin II heavy chain, and that F‐actin is not required for the maintenance of C DC4p and Myo 2p medial rings, suggesting that the attachment of CDC4pand Myo1p to the division site involves proteins other than actin itself.
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Tandem affinity purification and identification of protein complex components.
TL;DR: The tandem affinity purification or TAP approach combined with DALPC mass spectrometry is described to identify components of protein complexes as it has been applied to S. pombe to gain insight into functional protein assemblies and to elucidate functions of uncharacterized proteins.