Studies of pH regulation by Btn1p, the yeast homolog of human Cln3p.
Although the gene responsible for Batten disease, CLN3, was positionally cloned in 1995, the function of Cln3p and the molecular basis of the disease still remain elusive. We previously reported that the yeast Saccharomyces cerevisiae contains a homolog to Cln3p, designated Btn1p, and that the human Cln3p complemented the pH-dependent resistance to D-(-)-threo-2-amino-1-[p-nitrophenyl]-1, 3-propanediol in btn1-Delta yeast mutants. We have determined that yeast lacking Btn1p have an elevated ability to acidify media during growth that correlates with an elevated plasma membrane ATPase activity. Btn1p may be involved in maintaining pH homeostasis of yeast cells.
Pearce
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DA
Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA. David_Pearce@urmc.rochester.edu
Nosel
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SA
Sherman
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F
D002462:Cell Membrane / Q000378:metabolism; D016213:Cyclins / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D009472:Neuronal Ceroid-Lipofuscinoses / Q000209:etiology; D010641:Phenotype; D012441:Saccharomyces cerevisiae / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D013997:Time Factors
C079895:CLN3 protein, S cerevisiae; C105199:CLN3 protein, human; D016213:Cyclins; D005656:Fungal Proteins; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; C489809:YHC3 protein, S cerevisiae