Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1763, Issue 12, Pages 1613-1619Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2006.08.035
Keywords
importomer; docking and RING subcomplexes; peroxisomal matrix protein import
Categories
Funding
- NIDDK NIH HHS [R01 DK041737, DK41737, R37 DK041737-15, R37 DK041737] Funding Source: Medline
- NIGMS NIH HHS [GM59844] Funding Source: Medline
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The import of proteins into the peroxisome matrix is an essential step in peroxisome biogenesis, which is critical for normal functioning of most eukaryotic cells. The translocation of proteins across the peroxisome membrane and the dynamic behavior of the import receptors during the import cycle is facilitated by several peroxisome-membrane-associated protein complexes, one of which is called the importomer complex (B. Ague, N.M. Meindl, K. Niederhoff, H. Einwachter, P. Rehling, A. Sickmann, H.E. Meyer, W. Girzalsky, W.H. Kunau, Pex8p: an intraperoxisomal organizer of the peroxisomal import machinery, Mol. Cell 11 (2003) 635-646; P.P. Hazra, 1. Suriapranata, W.B. Snyder, S. Subramani, Peroxisome remnants in pex3 Delta, cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes, Traffic 3 (2002) 560-574. [1,2]]. We provide below a brief historical perspective regarding the importomer and its role in peroxisome biogenesis. We also identify areas in which further work is needed to uncover the physiological role of the importomer. (c) 2006 Elsevier B.V All rights reserved.
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