open access publication

Article, 2022

Transient accumulation and bidirectional movement of KIF13B in primary cilia

Journal of Cell Science, ISSN 1477-9137, 0021-9533, Volume 136, 5, 10.1242/jcs.259257

Contributors

Juhl, Alice Dupont [1] Anvarian, Zeinab [2] Kuhns, Stefanie 0000-0002-3065-7818 [1] Berges, Julia [2] [3] Andersen, Jens Skorstengaard 0000-0002-6091-140X [1] Wüstner, Daniel 0000-0003-4995-9709 [1] Pedersen, Lotte Bang 0000-0002-9749-3758 [2]

Affiliations

  1. [1] University of Southern Denmark
  2. [NORA names: SDU University of Southern Denmark; University; Denmark; Europe, EU; Nordic; OECD];
  3. [2] University of Copenhagen
  4. [NORA names: KU University of Copenhagen; University; Denmark; Europe, EU; Nordic; OECD];
  5. [3] Francisco de Vitoria University
  6. [NORA names: Spain; Europe, EU; OECD]

Abstract

Primary cilia are microtubule-based sensory organelles whose assembly and function rely on the conserved bidirectional intraflagellar transport (IFT) system, which is powered by anterograde kinesin-2 and retrograde cytoplasmic dynein-2 motors. Nematodes additionally employ a cell-type-specific kinesin-3 motor, KLP-6, which moves within cilia independently of IFT and regulates ciliary content and function. Here, we provide evidence that a KLP-6 homolog, KIF13B, undergoes bursts of bidirectional movement within primary cilia of cultured immortalized human retinal pigment epithelial (hTERT-RPE1) cells. Anterograde and retrograde intraciliary velocities of KIF13B were similar to those of IFT (as assayed using IFT172-eGFP), but intraciliary movement of KIF13B required its own motor domain and appeared to be cell-type specific. Our work provides the first demonstration of motor-driven, intraciliary movement by a vertebrate kinesin other than kinesin-2 motors.

Keywords

IFT, KIF13B, KLP-6, accumulation, anterograde, anterograde kinesin-2, assembly, bidirectional movement, burst, cell-type, cilia, content, demonstration, domain, dynein-2 motors, epithelial, evidence, function, homology, human retinal pigment epithelial, kinesin, kinesin-2, kinesin-2 motors, kinesin-3 motors, microtubule-based sensory organelles, motor, motor domain, motor-driven, movement, nematodes, organelles, pigment epithelial, primary cilia, regulating ciliary content, retinal pigment epithelial, sensory organelles, transient accumulation, vertebrates

Funders

  • Danish Cancer Society
  • Novo Nordisk Foundation
  • Novo Nordisk (Denmark)
  • European Commission
  • The Velux Foundations

Data Provider: Digital Science