ArticleMolecular biology of the cell2015
PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Decoding Rho GTPase signalling networks in directed cell migration.Frontiers in cell and developmental biology · 2026Review
- MARK2 regulates Golgi apparatus reorientation by phosphorylation of CAMSAP2 in directional cell migratio.eLife · 2025Article
- Analysis ofAnimals : an open access journal from MDPI · 2023Article
- Identification of CDC42 Effectors Operating in FGD1-Dependent Trafficking at the Golgi.Frontiers in cell and developmental biology · 2019Article
- Distinct Functions for Mammalian CLASP1 and -2 During Neurite and Axon Elongation.Frontiers in cellular neuroscience · 2019Article
- Rosiglitazone affects lumen formation in MDCKII cell through regulating apico-basal polarity.American journal of translational research · 2018Article
- Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein.Molecular & cellular proteomics : MCP · 2017Article
- Par3 integrates Tiam1 and phosphatidylinositol 3-kinase signaling to change apical membrane identity.Molecular biology of the cell · 2017Article
- PAR3-aPKC regulates Tiam1 by modulating suppressive internal interactions.Molecular biology of the cell · 2016Article
- Transport Vesicle Tethering at the Trans Golgi Network: Coiled Coil Proteins in Action.Frontiers in cell and developmental biology · 2016Review
- Par-3 modulates intestinal epithelial barrier function through regulating intracellular trafficking of occludin and myosin light chain phosphorylation.Journal of gastroenterology · 2015Article
- Nucleation and Dynamics of Golgi-derived Microtubules.Frontiers in neuroscience · 2015Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The organization of the Golgi apparatus is essential for cell polarization and its maintenance. The polarity regulator PAR complex (PAR3, PAR6, and aPKC) plays critical roles in several processes of cell polarization. However, how the PAR complex participates in regulating the organization of the Golgi remains largely unknown. Here we demonstrate the functional cross-talk of the PAR complex with CLASP2, which is a microtubule plus-end-tracking protein and is involved in organizing the Golgi ribbon. CLASP2 directly interacted with PAR3 and was phosphorylated by aPKC. In epithelial cells, knockdown of either PAR3 or aPKC induced the aberrant accumulation of CLASP2 at the trans-Golgi network (TGN) concomitantly with disruption of the Golgi ribbon organization. The expression of a CLASP2 mutant that inhibited the PAR3-CLASP2 interaction disrupted the organization of the Golgi ribbon. CLASP2 is known to localize to the TGN through its interaction with the TGN protein GCC185. This interaction was inhibited by the aPKC-mediated phosphorylation of CLASP2. Furthermore, the nonphosphorylatable mutant enhanced the colocalization of CLASP2 with GCC185, thereby perturbing the Golgi organization. On the basis of these observations, we propose that PAR3 and aPKC control the organization of the Golgi through CLASP2 phosphorylation.
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