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Plant and Cell Physiology, 1997, Vol. 38, No. 12 1414-1420
© 1997


Rapid Report

A Pumpkin 72-kDa Membrane Protein of Precursor-Accumulating Vesicles Has Characteristics of a Vacuolar Sorting Receptor

Tomoo Shimada1, Miwa Kuroyanagi1, Mikio Nishimura1,2 and Ikuko Hara-Nishimura1,2,3

1 Department of Cell Biology, National Institute for Basic Biology Okazaki, 444 Japan
2 Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies Okazaki, 444 Japan

3To whom correspondence should be addressed

Precursor-accumulating (PAC) vesicles were previously shown to mediate the transport of the precursor of a major storage protein (pro2S albumin) to protein-storage vacu-oles in developing pumpkin cotyledons. In this study, we characterized two homologous proteins from PAC vesicles, a 72 kDa protein (PV72) and an 82 kDa protein (PV82). PV72 and PV82 showed an ability to bind to peptides derived from both an internal propeptide and a C-terminal peptide of pro2S albumin. PV72 was predicted to be a type I integral membrane protein with epidermal growth factor (EGF)-like motifs. These results suggest that PV72 and PV82 are potential sorting receptors for 2S albumin to protein-storage vacuoles.

(Received August 25, 1997; Accepted October 17, 1997)
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