PKCε‐mediated phosphorylation of vimentin controls integrin recycling and motility

By J. Ivaska, Karoliina Vuoriluoto, T. Huovinen, I. Izawa, M. Inagaki, P. Parker. 2005

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Vimentin as a potential molecular target in cancer therapy Or Vimentin, an overview and its potential as a molecular target for cancer therapy (2011, unknown): “Vimentin was shown to promote cell motility in a protein kinase Ce (PKCe)-dependent manner and its phosphorylation by PKCe in integrin containing intracellular vesicles regulated its exit to the plasma membrane [ 62 ], suggesting a possible mechanism of its translocation to the plasma membrane.”
Vimentin regulates EMT induction by Slug and oncogenic H-Ras and migration by governing Axl expression in breast cancer (2011, background): “Moreover, overexpression of vimentin in a vimentin-negative, non-invasive MCF7 breast cancer cell line increases integrin traffic, migration and invasiveness (Hendrix et al., 1997; Ivaska et al., 2005).”
Derailed endocytosis: an emerging feature of cancer (2008, background): “For example, PKCe phosphorylates an intermediate filament protein, vimentin , thereby possibly releasing integrins from a mechanical tethe”
Structural Basis of Protein Kinase C Isoform Function (2008, background): “However, chronic PKC inhibition also leads to a defect in PKC -dependent phosphorylation of the intermediate filament protein vimentin (which is required for vesicular transport and protein trafficking) and the accumulation of PKC in large 1integrin-containing cytoplasmic vesicles, leading to abnorm”