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Updated: Jan 17, 2026

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
Published on: December 14, 2017
PKD3 localizes to late endosomes to maintain Rab7-dependent endolysosomal homeostasis
Elena Gutiérrez-Galindo1, Katharina Jursik1, Yannick Frey2
1Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
Abstract:
Protein kinase D3 (PKD3) is an important regulator of triple-negative breast cancer (TNBC) progression by promoting invasion, proliferation, and stem cell maintenance. However, the mechanism underlying these cellular functions has remained unclear. Here, we report that endogenous PKD3 localizes to Rab7-positive vesicles in MDA-MB-231 cells cultured on stiff matrices. Notably, PKD3 depletion results in smaller Rab7-positive vesicles with reduced retromer complex recruitment, leading to enhanced cathepsin D secretion. This correlates with impaired endosomal acidification, which is associated with dysregulated Wnt signaling and a decline in stemness. Our data thus unveil a previously unrecognized role of PKD3 in regulating endolysosomal dynamics that contributes to the maintenance of the cancer stem cell population in TNBC.
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