Kinectin-dependent ER transport supports the focal complex maturation required for chemotaxis in shallow gradients

J Cell Sci. 2016 Jul 1;129(13):2660-72. doi: 10.1242/jcs.181768. Epub 2016 May 24.

Abstract

Chemotaxis in shallow gradients of chemoattractants is accomplished by preferential maintenance of protrusions oriented towards the chemoattractant; however, the mechanism of preferential maintenance is not known. Here, we test the hypothesis that kinectin-dependent endoplasmic reticulum (ER) transport supports focal complex maturation to preferentially maintain correctly oriented protrusions. We knocked down kinectin expression in MDA-MB-231 cells using small interfering RNA and observed that kinectin contributes to the directional bias, but not the speed, of cell migration. Kymograph analysis revealed that the extension of protrusions oriented towards the chemoattractant was not affected by kinectin knockdown, but that their maintenance was. Immunofluorescence staining and live-cell imaging demonstrated that kinectin transports ER preferentially to protrusions oriented towards the chemoattractant. ER then promotes the maturation of focal complexes into focal adhesions to maintain these protrusions for chemotaxis. Our results show that kinectin-dependent ER distribution can be localized by chemoattractants and provide a mechanism for biased protrusion choices during chemotaxis in shallow gradients of chemoattractants.

Keywords: Chemotaxis; Endoplasmic reticulum; Focal complex maturation; Kinectin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Cell Movement / genetics*
  • Chemotactic Factors / genetics
  • Chemotactic Factors / metabolism
  • Chemotaxis / genetics*
  • Endoplasmic Reticulum / genetics*
  • Endoplasmic Reticulum / metabolism
  • Focal Adhesions / genetics
  • Focal Adhesions / metabolism
  • Gene Expression Regulation
  • Gene Knockdown Techniques
  • Humans
  • Kymography
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism

Substances

  • Chemotactic Factors
  • KTN1 protein, human
  • Membrane Proteins