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The N-terminal signal peptide of the murine cyclophilin mCyP-S1 is required in vivo for ER localization

Title data

Schumacher, A. ; Westermann, Benedikt ; Osborn, M. ; Nordheim, A.:
The N-terminal signal peptide of the murine cyclophilin mCyP-S1 is required in vivo for ER localization.
In: European Journal of Cell Biology. Vol. 63 (1994) Issue 2 . - pp. 182-191.
ISSN 1618-1298

Abstract in another language

Cyclophilins are a class of enzymes that are thought to be involved in protein folding by accelerating the isomerization of Xaa-Pro peptide bonds and that mediate the immunosuppressive effect of cyclosporin A. We described previously a murine cyclophilin, mCyP-S1, whose cDNA encoded a putative NH2-terminal signal sequence which was not present in the mature protein. Here we investigate the intracellular localization of mCyP-S1. We show by overexpression of the wild-type and an NH2-terminally truncated derivative that its signal sequence is necessary and functional in vivo for the translocation into the endoplasmic reticulum (ER). Immunocytochemistry and cell fractionations demonstrate the preferential localization of endogenous mCyP-S1 in the ER, or subcompartments thereof. In addition, the results indicate the presence of this cyclophilin in the nucleus.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Professor Cell Biology > Professor Cell Biology - Univ.-Prof. Dr. Benedikt Westermann
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Professor Cell Biology
Result of work at the UBT: No
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 15 Oct 2020 11:20
Last Modified: 06 Jun 2023 11:23
URI: https://eref.uni-bayreuth.de/id/eprint/58357