Rac regulates the interaction of fascin with protein kinase C in cell migration

Parsons, Maddy; Adams, Josephine C.

doi:10.1242/jcs.022509

Cited by 67 publications

(69 citation statements)

References 49 publications

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“…Small GTPases of the Rho family, including Rac1, can activate fascin in vitro (Adams and Schwartz, 2000;Hashimoto et al, 2007;Parsons and Adams, 2008). Furthermore, overexpression of Rac1 can induce the formation of extra filopodia in class III neurons (Andersen et al, 2005;Lee et al, 2003) (supplementary material Fig.…”

Section: Singed Activity Is Modulated By Phosphorylationmentioning

confidence: 99%

Fascin controls neuronal class-specific dendrite arbor morphology

et al. 2012

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SUMMARYThe branched morphology of dendrites represents a functional hallmark of distinct neuronal types. Nonetheless, how diverse neuronal class-specific dendrite branches are generated is not understood. We investigated specific classes of sensory neurons of Drosophila larvae to address the fundamental mechanisms underlying the formation of distinct branch types. We addressed the function of fascin, a conserved actin-bundling protein involved in filopodium formation, in class III and class IV sensory neurons. We found that the terminal branchlets of different classes of neurons have distinctive dynamics and are formed on the basis of molecularly separable mechanisms; in particular, class III neurons require fascin for terminal branching whereas class IV neurons do not. In class III neurons, fascin controls the formation and dynamics of terminal branchlets. Previous studies have shown that transcription factor combinations define dendrite patterns; we find that fascin represents a downstream component of such programs, as it is a major effector of the transcription factor Cut in defining class III-specific dendrite morphology. Furthermore, fascin defines the morphological distinction between class III and class IV neurons. In fact, loss of fascin function leads to a partial conversion of class III neurons to class IV characteristics, while the reverse effect is obtained by fascin overexpression in class IV neurons. We propose that dedicated molecular mechanisms underlie the formation and dynamics of distinct dendrite branch types to elicit the accurate establishment of neuronal circuits.

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Section: Singed Activity Is Modulated By Phosphorylationmentioning

confidence: 99%

Fascin controls neuronal class-specific dendrite arbor morphology

et al. 2012

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“…Fascin-1 (Vignjevic et al, 2007;Parsons and Adams, 2008). Upregulation of Fascin-1 within the actin-cytoskeleton pathway is thought to promote the migratory potential and, therefore, the invasive phenotype of malignant cancer cells, which can ultimately lead to metastasis (Vignjevic et al, 2007).…”

Section: Figmentioning

confidence: 99%

The Actin-Cytoskeleton Pathway and Its Potential Role in Inflammatory Bowel Disease-Associated Human Colorectal Cancer

Kanaan

Qadan

Eichenberger

et al. 2010

Genetic Testing and Molecular Biomarkers

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“…Among the dedifferentiated cell lines representing highly advanced cancer, Lovo and SW480 cells were conspicuous for constitutively expressing high levels of nonphosphorylated as well as Thr 514 -phosphorylated PKCγ. Although, the expression level of PKCγ was lower in DLD-1 cells than in SW480 and Lovo, in a previous study it was stated that PKCγ was the major conventional PKC in DLD-1 cells [29].…”

Section: Discussionmentioning

confidence: 79%

“…PKCγ and PKCδ were reported to be involved in insulin-like growth factor I-induced migration in colonic epithelial cells [40]. Furthermore, in protrusions and filipodia of migrating SW480 cells, PKCγ interacted with fascin, an actin-binding protein which is low or absent in normal colonic epithelia [29]. The results of the present study appear to be consistent with such a role of PKCγ, as it was detected at higher levels in cell lines derived from advanced or metastatic colon cancer cells.…”

Section: Discussionmentioning

confidence: 99%

“…In reviews on PKC isoenzymes in colon carcinogenesis, PKCγ was not discussed either among the isoforms expressed in normal enterocytes and colonocytes, or among the PKC isoforms which play a role in cancer development [5,36]. However, in a recent study with SW480 colon carcinoma cells, it was mentioned that in SW480, SW1222 and DLD-1 cells, PKCγ was expressed as the major conventional PKC [29]. Our study with a set of different colon cancer cell lines gives to some extent an explanation of this apparent discrepancy by demonstrating the colon cancer cell type-specific expression of PKCγ, which can be detected at higher expression levels in some dedifferentiated colon cancer cell lines (Lovo, SW480), or under butyrate treatment (HT29), or when probed with an antibody against its phospho-Thr 514 -modified-form (Caco2 and IEC-18).…”

Section: Discussionmentioning

confidence: 99%

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Protein kinase Cγ in colon cancer cells: Expression, Thr514 phosphorylation and sensitivity to butyrate-mediated upregulation as related to the degree of differentiation

Garczarczyk

Szekér

Gálfi

et al. 2010

Chemico-Biological Interactions

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Protein kinase C (PKC) isoenzymes are expressed and activated in a cell type-specific manner, and play an essential role in tissue-specific signal transduction. The presence of butyrate at millimolar concentrations in the colon raises the question of whether it affects the expression of PKC isoenzymes in the different cell types of the colonic epithelium. We investigated the protein expression levels of PKCγ, Thr 514 -phosphorylated PKCγ (pPKCγ-Thr 514 ), and their subcellular distribution as affected by butyrate in a set of colon cancer cell lines. Thr 514 -phosphorylation of de novo synthesized PKCγ is the first step in priming of the inactive PKCγ before its release into the cytoplasm. For immunoblot analysis, we employed three antibodies, one against an unmodified sequence, mapping within 50 amino acids at its C-terminus, a second against pPKCγ-Thr 514 , and a third against pPKCγ-pan-Thr 514 . The antibody against an unmodified C-terminal peptide epitope did not recognize pPKCγ-Thr 514 , suggesting that phosphorylation at this site interferes with the binding of the antibody to the C-terminus. Marked butyrate-induced upregulation of PKCγ occurred in HT29 cells (colonocyte stem cells) and HT29-derived cell lines. However, in Caco2 and IEC-18 cells (differentiated intestinal epithelial cells), PKCγ was insensitive to upregulation, and present exclusively as pPKCγ-Thr 514 . Lovo and SW480 expressed higher levels of PKCγ. In HT29 cells, butyrate-induced upregulation of the non-phosphorylated PKCγ was observed in both the membrane and cytosolic fraction. In Caco2 cells, the Thr 514 -phosphorylated form was present at high levels in both fractions. The presence of unphosphorylated PKCγ in HT29 cells, and its complete absence in Caco2 cells demonstrates a cell type-dependent differential coupling of Thr 514 -phosphorylation with de novo synthesis of PKCγ in colon cancer cells.

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Rac regulates the interaction of fascin with protein kinase C in cell migration

Cited by 67 publications

References 49 publications

Fascin controls neuronal class-specific dendrite arbor morphology

Fascin controls neuronal class-specific dendrite arbor morphology

The Actin-Cytoskeleton Pathway and Its Potential Role in Inflammatory Bowel Disease-Associated Human Colorectal Cancer

Protein kinase Cγ in colon cancer cells: Expression, Thr514 phosphorylation and sensitivity to butyrate-mediated upregulation as related to the degree of differentiation

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