Work

Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole

Year: 2000

Type: article

Abstract: Eukaryotic 70 kDa heat shock proteins (Hsp70s) are localized in various cellular compartments and exhibit functions such as protein translocation across membranes, protein folding and assembly. Here we demonstrate that the constitutively expressed members of the yeast cytoplasmic Ssa subfamily, Ssa1/2p, are involved in the transport of the vacuolar hydrolase aminopeptidase 1 from the cytoplasm into the vacuole. The Ssap family members displayed overlapping functions in the transport of aminopeptidase 1. In SSAI and SSAII deletion mutants the precursor of aminopeptidase 1 accumulated in a dodecameric complex that is packaged in prevacuolar transport vesicles. Ssa1/2p was prominently localized to the vacuolar membrane, consistent with the role we propose for Ssa proteins in the fusion of transport vesicles with the vacuolar membrane.

Source: FEBS Letters

DOI: 10.1016/s0014-5793(00)01324-7

Authors: Chitkala Satyanarayana, Stephan Schröder-Köhne, Elizabeth A. Craig, Peter V. Schu, Martin Horst

Institutions: University of Göttingen, Max Planck Institute for Biophysical Chemistry, University of Wisconsin–Madison

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: Deutsche Forschungsgemeinschaft

OpenAlex ID: W2003076943

FWCI: 0.845

Cites: 43

Cited by: 23

Related to: 10