Structure and Function of Dynein’s Non-Catalytic Subunits

Research output: Contribution to journalReview articlepeer-review

Abstract

Dynein, an ancient microtubule-based motor protein, performs diverse cellular functions in nearly all eukaryotic cells, with the exception of land plants. It has evolved into three subfamilies—cytoplasmic dynein-1, cytoplasmic dynein-2, and axonemal dyneins—each differentiated by their cellular functions. These megadalton complexes consist of multiple subunits, with the heavy chain being the largest subunit that generates motion and force along microtubules by converting the chemical energy of ATP hydrolysis into mechanical work. Beyond this catalytic core, the functionality of dynein is significantly enhanced by numerous non-catalytic subunits. These subunits are integral to the complex, contributing to its stability, regulating its enzymatic activities, targeting it to specific cellular locations, and mediating its interactions with other cofactors. The diversity of non-catalytic subunits expands dynein’s cellular roles, enabling it to perform critical tasks despite the conservation of its heavy chains. In this review, we discuss recent findings and insights regarding these non-catalytic subunits.

Original languageEnglish (US)
Article number330
JournalCells
Volume13
Issue number4
DOIs
StatePublished - Feb 2024

Keywords

  • axonemal dynein
  • cytoplasmic dynein-1
  • cytoplasmic dynein-2
  • intermediate chain
  • light chain
  • light intermediate chain
  • microtubules
  • molecular motors

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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