Cell Biology and Membrane Transport Processes by Michael Caplan (Eds.)

By Michael Caplan (Eds.)

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Kane, I. Pastan, and M. M. Gottesman, unpublished observations). Why does the transporter contain two ATP-binding regions, and is ATP really the preferred energy source for transport? Currently, the first of these questions is unanswered, but several hypotheses may be entertained. One of the sites may be regulatory, and the second could be catalytic. Both sites might be needed because the first gets the substrate into the transporter, and the second gets it out (I. Roninson, personal communication).

INTRODUCTION In eukaryotic cells, the vast majority of peptide hormones and other polypeptides destined for secretion are typically synthesized as larger precursors on cytoplasmic polysomes and then targeted to the membrane ' Current address: Department of Molecular Genetics and the Biocenter, University of Vienna, Dr. Bohrgasse 9/2, A-1030, Vienna, Austria. Current Topics in Membranes, Volume 41 Copyright 0 1994 by Academic Press, Inc. All rights of reproduction in any form reserved. 19 20 Karl Kuchler et af.

Like the other members of the family that are above 100,000 kDa, Ste6p is predicted from its sequence to have two discrete ABC domains. Hydrolysis of ATP has been shown to energize the transport process mediated by the highly related transporter, Mdrl (Hamada and Tsuruo, 1988)and by other members of this superfam- 2. Transmembrane Translocation of Peptides 21 ily (for reviews see Higgins, 1992; Kuchler and Thorner, 1992a). , 1993a). This cross-linking was specific to Ste6p because no labeled species was detectable in cells not expressing Ste6p, because appearance of the photolabeled 145-kDa product required UV-irradiation, and because labeling was effectively competed by the presence of excess unlabeled nucleotide.

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