Role of fission yeast myosin I in organization of sterol-rich membrane domains

Tetsuya Takeda, Fred Chang

Research output: Contribution to journalArticlepeer-review

47 Citations (Scopus)


Specialized membrane domains containing lipid rafts are thought to be important for membrane processes such as signaling and trafficking [1, 2]. An unconventional type I myosin has been shown to reside in lipid rafts and function to target a disaccharidase to rafts in brush borders of intestinal mammalian cells [3]. In the fission yeast Schizosaccharomyces pombe, distinct sterol-rich membrane domains are formed at the cell division site and sites of polarized cell growth at cell tips [4]. Here, we show that the sole S. pombe myosin I, myo1p, is required for proper organization of these membrane domains. myo1 mutants lacking the TH1 domain exhibit a uniform distribution of sterol-rich membranes all over the plasma membrane throughout the cell cycle. These effects are independent of endocytosis because myo1 mutants exhibit no endocytic defects. Conversely, overexpression of myo1p induces ectopic sterol-rich membrane domains. Myo1p localizes to nonmotile foci that cluster in sterol-rich plasma membrane domains and fractionates with detergent-resistant membranes. Because the myo1p TH1 domain may bind directly to acidic phospholipids, these findings suggest a model for how type I myosin contributes to the organization of specialized membrane domains.

Original languageEnglish
Pages (from-to)1331-1336
Number of pages6
JournalCurrent Biology
Issue number14
Publication statusPublished - Jul 26 2005
Externally publishedYes

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology
  • General Agricultural and Biological Sciences


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