ArticleThe Journal of biological chemistry2009
Phosphorylation of alpha6-tubulin by protein kinase Calpha activates motility of human breast cells.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- How phosphorylation of α/β-tubulin perturbs microtubule structure: A computational study.The Journal of biological chemistry · 2026Article
- Emerging Roles of Tubulin Isoforms and Their Post-Translational Modifications in Microtubule-Based Transport and Cellular Functions.Biomolecules · 2026Review
- Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Distinct features of the host-parasite interactions between nonadherent and adherent Trichomonas vaginalis isolates.PLoS neglected tropical diseases · 2023Article
- SILAC kinase screen identifies potential MASTL substrates.Scientific reports · 2022Article
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Intrinsic and Extrinsic Factors Affecting Microtubule Dynamics in Normal and Cancer Cells.Molecules (Basel, Switzerland) · 2020Review
- Phosphorylation state of SerCellular signalling · 2018Article
- Tubulin Post-Translational Modifications and Microtubule Dynamics.International journal of molecular sciences · 2017Review
- Protein kinase C in cancer: The top five unanswered questions.Molecular carcinogenesis · 2017Review
- A conserved region within interferon regulatory factor 5 controls breast cancer cell migration through a cytoplasmic and transcription-independent mechanism.Molecular cancer · 2015Article
- Phosphorylation of Cdc42 effector protein-4 (CEP4) by protein kinase C promotes motility of human breast cells.The Journal of biological chemistry · 2014Article
- Phosphorylation of α-tubulin by protein kinase C stimulates microtubule dynamics in human breast cells.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Analysis of substrates of protein kinase C isoforms in human breast cells by the traceable kinase method.Biochemistry · 2012Article
- PKCα regulates vasopressin-induced aquaporin-2 trafficking in mouse kidney collecting duct cells in vitro via altering microtubule assembly.Acta pharmacologica Sinica · 2012Article
- Acquiring Metastatic Competence by Oral Squamous Cell Carcinoma Cells Is Associated with Differential Expression of α-Tubulin Isoforms.Journal of oncology · 2012Article
- Adhesion of Trypanosoma cruzi trypomastigotes to fibronectin or laminin modifies tubulin and paraflagellar rod protein phosphorylation.PloS one · 2012Article
- Protein kinase Cα promotes cell migration through a PDZ-dependent interaction with its novel substrate discs large homolog 1 (DLG1).The Journal of biological chemistry · 2011Article
- Migration of MDA-MB-231 breast cancer cells depends on the availability of exogenous lipids and cholesterol esterification.Clinical & experimental metastasis · 2011Article
- CSPG4 protein as a new target for the antibody-based immunotherapy of triple-negative breast cancer.Journal of the National Cancer Institute · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Engineered overexpression of protein kinase Calpha (PKCalpha) was previously shown to endow nonmotile MCF-10A human breast cells with aggressive motility. A traceable mutant of PKCalpha (Abeyweera, T. P., and Rotenberg, S. A. (2007) Biochemistry 46, 2364-2370) revealed that alpha6-tubulin is phosphorylated in cells expressing traceable PKCalpha and in vitro by wild type PKCalpha. Gain-of-function, single site mutations (Ser-->Asp) were constructed at each PKC consensus site in alpha6-tubulin (Ser158, Ser165, Ser241, and Thr337) to simulate phosphorylation. Following expression of each construct in MCF-10A cells, motility assays identified Ser165 as the only site in alpha6-tubulin whose pseudophosphorylation reproduced the motile behavior engendered by PKCalpha. Expression of a phosphorylation-resistant mutant (S165N-alpha6-tubulin) resulted in suppression of MCF-10A cell motility stimulated either by expression of PKCalpha or by treatment with PKCalpha-selective activator diacylglycerol-lactone. MCF-10A cells treated with diacylglycerol-lactone showed strong phosphorylation of endogenous alpha-tubulin that could be blocked when S165N-alpha6-tubulin was expressed. The S165N mutant also inhibited intrinsically motile human breast tumor cells that express high endogenous PKCalpha levels (MDA-MB-231 cells) or lack PKCalpha and other conventional isoforms (MDA-MB-468 cells). Comparison of Myc-tagged wild type alpha6-tubulin and S165N-alpha6-tubulin expressed in MDA-MB-468 cells demonstrated that Ser165 is also a major site of phosphorylation for endogenously active, nonconventional PKC isoforms. PKC-stimulated motility of MCF-10A cells was nocodazole-sensitive, thereby implicating microtubule elongation in the mechanism. These findings support a model in which PKC phosphorylates alpha-tubulin at Ser165, leading to microtubule elongation and motility.
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