Trans-Golgi network morphology and sorting is regulated by prolyl-oligopeptidase-like protein PREPL and the AP-1 complex subunit mu 1A
2013 | journal article. A publication with affiliation to the University of Göttingen.
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Trans-Golgi network morphology and sorting is regulated by prolyl-oligopeptidase-like protein PREPL and the AP-1 complex subunit mu 1A
Radhakrishnan, K.; Baltes, J.; Creemers, J. W. M. & Schu, P. (2013)
Journal of Cell Science, 126(5) pp. 1155-1163. DOI: https://doi.org/10.1242/jcs.116079
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- Authors
- Radhakrishnan, Karthikeyan; Baltes, Jennifer; Creemers, John W. M.; Schu, Peter
- Abstract
- The AP-1 complex recycles between membranes and the cytoplasm and dissociates from membranes during clathrin-coated-vesicle uncoating, but also independently of vesicular transport. The mu 1A N-terminal 70 amino acids are involved in regulating AP-1 recycling. In a yeast two-hybrid library screen we identified the cytoplasmic prolyl-oligopeptidase-like protein PREPL as an interaction partner of this domain. PREPL overexpression leads to reduced AP-1 membrane binding, whereas reduced PREPL expression increases membrane binding and impairs AP-1 recycling. Altered AP-1 membrane binding in PREPL-deficient cells mirrors the membrane binding of the mutant AP-1 complex, which is not able to bind PREPL. Colocalisation of PREPL with residual membrane-bound AP-1 can be demonstrated. Patient cell lines deficient in PREPL have an expanded trans-Golgi network, which could be rescued by PREPL expression. These data demonstrate PREPL as an AP-1 effector that takes part in the regulation of AP-1 membrane binding. PREPL is highly expressed in brain and at lower levels in muscle and kidney. Its deficiency causes hypotonia and growth hormone hyposecretion, supporting essential PREPL functions in AP-1-dependent secretory pathways.
- Issue Date
- 2013
- Status
- published
- Publisher
- Company Of Biologists Ltd
- Journal
- Journal of Cell Science
- ISSN
- 0021-9533