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Taking a lipidation-dependent path toward endolysosomes. | LitMetric

Taking a lipidation-dependent path toward endolysosomes.

Commun Integr Biol

Department of Chemical and Physical Biology; Centro de Investigaciones Biológicas, CSIC ; Madrid, Spain.

Published: April 2016

AI Article Synopsis

  • * Researchers created chimeric fluorescent proteins containing the CINCCKVL sequence, which effectively mark endolysosomes without altering their shape, unlike other commonly used fluorescent markers that can cause unwanted cell structure changes.
  • * The findings suggest that the lipidation-dependent localization of these CINCCKVL chimeras to endolysosomes is a conserved process among various cell types, making them valuable tools for studying these cellular compartments.

Article Abstract

We recently reported that the isoprenylation and palmitoylation motif present at the C-terminus of human RhoB protein promotes intraluminal vesicle delivery of proteins in cells from organisms as phylogenetically apart as fungi and humans. Here we build on these observations by showing that chimeras of fluorescent proteins bearing this sequence, namely, CINCCKVL, which become isoprenylated and palmitoylated in cells, may be used to mark endolysosomes while preserving their morphology. Indeed, these chimeric proteins are devoid of the effects derived from overexpression of fluorescent constructs of full-length, active proteins widely used as endolysosomal markers, such as Lamp1 or Rab7, which cause lysosomal enlargement, or RhoB, which induces actin stress fibers. Moreover, the fact that lipidation-dependent endolysosomal localization of CINCCKVL chimeras can be ascertained in a wide variety of cells indicates that they follow a path toward endolysosomes that is conserved in diverse species. Therefore, CINCCKVL chimeras serve as robust tools to mark these late endocytic compartments.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802854PMC
http://dx.doi.org/10.1080/19420889.2015.1078041DOI Listing

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