Molecular Basis for Selectivity & Transport in Ion Pumps

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 5R01GM052414-03
• Application #: 2899288
• Project Start: 1998-01-01
• Project End: 1998-08-31
• Support Year: 3
• Fiscal Year: 1999

Publications

Patenaude, Cassandra; Zhang, Yongqiang; Cormack, Brendan et al. (2013) Essential role for vacuolar acidification in Candida albicans virulence. J Biol Chem 288:26256-64

Leitch, Sharon; Feng, Mingye; Muend, Sabina et al. (2011) Vesicular distribution of Secretory Pathway Ca²+-ATPase isoform 1 and a role in manganese detoxification in liver-derived polarized cells. Biometals 24:159-70

Wei, Y; Chen, J; Rosas, G et al. (2000) Phenotypic screening of mutations in Pmr1, the yeast secretory pathway Ca2+/Mn2+-ATPase, reveals residues critical for ion selectivity and transport. J Biol Chem 275:23927-32

Mandal, D; Woolf, T B; Rao, R (2000) Manganese selectivity of pmr1, the yeast secretory pathway ion pump, is defined by residue gln783 in transmembrane segment 6. Residue Asp778 is essential for cation transport. J Biol Chem 275:23933-8

Marchi, V; Sorin, A; Wei, Y et al. (1999) Induction of vacuolar Ca2+-ATPase and H+/Ca2+ exchange activity in yeast mutants lacking Pmr1, the Golgi Ca2+-ATPase. FEBS Lett 454:181-6