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Vol. 9, Issue 5, 1149-1162, May 1998
Institut für Biochemie der Universität Stuttgart,
D-70569 Stuttgart, Germany; and
The yeast Ca2+ adenosine triphosphatase Pmr1, located
in medial-Golgi, has been implicated in intracellular
transport of Ca2+ and Mn2+ ions. We show here
that addition of Mn2+ greatly alleviates defects of
pmr1 mutants in N-linked and O-linked protein
glycosylation. In contrast, accurate sorting of carboxypeptidase Y
(CpY) to the vacuole requires a sufficient supply of intralumenal Ca2+. Most remarkably, pmr1 mutants are also
unable to degrade CpY*, a misfolded soluble endoplasmic reticulum
protein, and display phenotypes similar to mutants defective in the
stress response to malfolded endoplasmic reticulum proteins. Growth
inhibition of pmr1 mutants on Ca2+-deficient
media is overcome by expression of other Ca2+ pumps,
including a SERCA-type Ca2+ adenosine triphosphatase from
rabbit, or by Vps10, a sorting receptor guiding non-native luminal
proteins to the vacuole. Our analysis corroborates the dual function of
Pmr1 in Ca2+ and Mn2+ transport and establishes
a novel role of this secretory pathway pump in endoplasmic
reticulum-associated processes.
Laboratoire de
Biophysique Moléculaire et Cellulaire, Département de
Biologie Moléculaire et Structurale, Centre d'Etudes
Nucléaires de Grenoble, 38054 Grenoble Cedex 9, France
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