ArticleMolecular biology of the cell2016
PAR3-aPKC regulates Tiam1 by modulating suppressive internal interactions.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Retinal ribbon synapses and the potential functional role of TIAM1: A structural and molecular perspective.Molecular vision · 2026Review
- Apical-basal polarity and the control of epithelial form and function.Nature reviews. Molecular cell biology · 2022Review
- A MZB Cell Activation Profile Present in the Lacrimal Glands of Sjögren's Syndrome-Susceptible C57BL/6.NOD-International journal of molecular sciences · 2022Article
- The polarity protein PARD3 and cancer.Oncogene · 2021Review
- The N-terminal domain of the adaptor protein p140Cap interacts with Tiam1 and controls Tiam1/Rac1 axis.American journal of cancer research · 2020Article
- Targeting Rac and Cdc42 GEFs in Metastatic Cancer.Frontiers in cell and developmental biology · 2020Review
- Tiam1 is Critical for Glutamatergic Synapse Structure and Function in the Hippocampus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Polarization and sprouting of endothelial cells by angiopoietin-1 require PAK2 and paxillin-dependent Cdc42 activation.Molecular biology of the cell · 2019Article
- Mesenchymal-epithelial transition in development and reprogramming.Nature cell biology · 2019Review
- PAR3-PAR6-atypical PKC polarity complex proteins in neuronal polarization.Cellular and molecular life sciences : CMLS · 2018Review
- The Tiam1 guanine nucleotide exchange factor is auto-inhibited by its pleckstrin homology coiled-coil extension domain.The Journal of biological chemistry · 2017Article
- TIAM1 variants improve clinical outcome in neuroblastoma.Oncotarget · 2017Article
- Discovery of long-range inhibitory signaling to ensure single axon formation.Nature communications · 2017Article
- Par3 integrates Tiam1 and phosphatidylinositol 3-kinase signaling to change apical membrane identity.Molecular biology of the cell · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tiam1 is one of the most extensively analyzed activators of the small GTPase Rac. However, fundamental aspects of its regulation are poorly understood. Here we demonstrate that Tiam1 is functionally suppressed by internal interactions and that the PAR complex participates in its full activation. The N-terminal region of Tiam1 binds to the protein-binding and catalytic domains to inhibit its localization and activation. Atypical PKCs phosphorylate Tiam1 to relieve its intramolecular interactions, and the subsequent stabilization of its interaction with PAR3 allows it to exert localized activity. By analyzing Tiam1 regulation by PAR3-aPKC within the context of PDGF signaling, we also show that PAR3 directly binds PDGF receptor β. Thus we provide the first evidence for the negative regulation of Tiam1 by internal interactions, elucidate the nature of Tiam1 regulation by the PAR complex, and reveal a novel role for the PAR complex in PDGF signaling.
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