Literature DB >> 34463521

A WICB 50th Favorite: A conserved mechanism for mitochondria-dependent dynein anchoring.

Jenna R Christensen1.   

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Year:  2021        PMID: 34463521      PMCID: PMC8684709          DOI: 10.1091/mbc.E21-04-0217

Source DB:  PubMed          Journal:  Mol Biol Cell        ISSN: 1059-1524            Impact factor:   4.138


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To celebrate the 50th anniversary of the American Society for Cell Biology's Women in Cell Biology Committee (WICB), members of WICB and the MBoC Editorial Board invited a diverse group of scientists to highlight MBoC papers by women that have had a scientific or personal impact on the authors of the highlight. How is the same protein adapted by different organisms? This elegant work from Kraft and Lackner (2019) embodies one of my favorite types of papers to read—the authors use a thoughtful comparative cell biology approach to obtain keen mechanistic insight on cellular organization. The focus is Num1, a protein previously discovered in Saccharomyces cerevisiae to link the mitochondria, endoplasmic reticulum, and dynein at the cell cortex. An evolutionarily distant yeast, Schizosaccharomyces pombe, also has a Num1 homologue that functions solely in meiosis. Here, the authors find that Num1 from S. pombe also anchors mitochondria to the plasma membrane and recruits dynein to those sites. Perhaps just as intriguing as the similarities in Num1 function observed, they find differences between Num1’s roles in S. pombe and S. cerevisiae. The endoplasmic reticulum is not present at mitochondria/dynein interaction points in S. pombe, suggesting that the functionality of Num1 and the formation of these contact sites may still differ in some respects between these two yeasts.
  1 in total

1.  A conserved mechanism for mitochondria-dependent dynein anchoring.

Authors:  Lauren M Kraft; Laura L Lackner
Journal:  Mol Biol Cell       Date:  2019-01-16       Impact factor: 4.138

  1 in total

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