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Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways
By filtering chemical-genetic profiles for the multidrug-resistant genes and then clustering the compound-specific profiles with a compendium of large-scale genetic interaction profiles, this method provides a powerful means for inferring mechanism of action.
The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase
- P. Kane
- BiologyMicrobiology and Molecular Biology Reviews
- 1 March 2006
Current knowledge of the structure, function, and regulation of the V- ATPase in S. cerevisiae is discussed and the relationship between biosynthesis and transport of V-ATPase and compartment-specific regulation of acidification is examined.
The yeast lysosome-like vacuole: endpoint and crossroads.
Vacuolar and Plasma Membrane Proton Pumps Collaborate to Achieve Cytosolic pH Homeostasis in Yeast*
- Gloria A Martínez-Muñoz, P. Kane
- Biology, Environmental ScienceJournal of Biological Chemistry
- 18 July 2008
It is proposed that short-term, V-ATPase activity is essential for both vacuolar acidification in response to glucose metabolism and for efficient cytosolic pH homeostasis, and long-term.
Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo.
- P. Kane
- BiologyThe Journal of biological chemistry
- 14 July 1995
The H Subunit (Vma13p) of the Yeast V-ATPase Inhibits the ATPase Activity of Cytosolic V1 Complexes*
The results indicate that the H subunit plays an important role in silencing unproductive ATP hydrolysis by cytosolic V1 complexes, but suggest that other mechanisms, such as product inhibition, may also play a role insilencing in vivo.
The signaling lipid PI(3,5)P2 stabilizes V1–Vo sector interactions and activates the V-ATPase
Purified Vo complexes bind preferentially to this lipid, and the cytosolic domain of one Vo subunit shows PI(3,5)P2-dependent recruitment to membranes in vivo.
Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase.
- P. Kane, C. Yamashiro, D. F. Wolczyk, N. Neff, M. Goebl, T. Stevens
- Biology, Computer ScienceScience
- 2 November 1990
Evidence is presented that both the 69-kilodalton (kD) catalytic subunit of the vacuolar proton-translocating adenosine triphosphatase (H(+)-ATPase) and a 50-kD protein are obtained from a single translation product that is cleaved to release the 50- kD protein and spliced to form the 69 -kD subunit.
The RAVE Complex Is Essential for Stable Assembly of the Yeast V-ATPase*
- A. Smardon, Maureen Tarsio, P. Kane
- Biology, ChemistryThe Journal of Biological Chemistry
- 19 April 2002
Evidence supporting a role for RAVE in reassembly of the V-ATPase is provided but also an essential role in V- ATPase assembly under other conditions is demonstrated.
Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase
- C. Yamashiro, P. Kane, D. F. Wolczyk, R. Preston, T. Stevens
- Environmental Science, BiologyMolecular and cellular biology
- 1 July 1990
The results indicate that the vacuolar proton-translocating ATPase complex is essential for vacUolar acidification and that the low-pH state of the vacUole is crucial for normal growth.