Mitochondrial protein-import machinery: correlating structure with function

Author(s): Baker, MJ; Frazier, AE; Gulbis, JM; Ryan, MT;
Details: Publication Year 2007-09,Volume 17,Issue #9,Page 456-464
Journal Title: TRENDS IN CELL BIOLOGY
Publication Type: Journal Article
Abstract: Most mitochondriall proteins are synthesized in the cytosol, translocated into the organelle and directed along specific sorting pathways. Over the past 20 years, >30 proteins have been identified as having key roles in mitochondrial protein import. Recently, the elucidation of the structures of several import components has provided fresh insight into the import process. Here, we review the different pathways involved in sorting proteins into mitochondrial subcompartments. Along the way, we highlight the available structural information about the protein-import machinery and discuss how these structures correlate with previously ascribed functions. Future challenges for the cell biologists will be to use this structural information to test specific hypotheses addressing the molecular mechanisms of mitochondrial protein import.
Publisher: ELSEVIER SCIENCE LONDON
Keywords: INTERMEMBRANE SPACE PROTEINS; DEPENDENT SULFHYDRYL OXIDASE; TIM23 PREPROTEIN TRANSLOCASE; CYTOCHROME BC(1) COMPLEX; CRYSTAL-STRUCTURE; OUTER-MEMBRANE; INNER MEMBRANE; PRESEQUENCE TRANSLOCASE; ADP/ATP CARRIER; J-DOMAIN
Publisher's Version: https://doi.org/10.1016/j.tcb.2007.07.010
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2007-09-01 12:00:00