TIAM-1/GEF can shape somatosensory dendrites independently of its GEF activity by regulating F-actin localization
| Autor: | Leo T.H. Tang, Nelson J. Ramirez-Suarez, Carlos A. Díaz-Balzac, María I. Lázaro-Peña, Maisha Rahman, Hannes E. Bülow, Yehuda Salzberg |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
rac1 GTP-Binding Protein
PDZ Domains Nervous System Synaptic Transmission 0302 clinical medicine guanine nucleotide exchange factor T-Lymphoma Invasion and Metastasis-inducing Protein 1 Biology (General) Caenorhabditis elegans Neurons 0303 health sciences Neuronal Plasticity biology Chemistry General Neuroscience General Medicine Transmembrane protein Cell biology Protein Transport medicine.anatomical_structure C. elegans Medicine Guanine nucleotide exchange factor actin Intracellular Research Article Protein Binding GEF independent dendrites QH301-705.5 Neurogenesis Science PDZ domain Dendrite RAC1 General Biochemistry Genetics and Molecular Biology 03 medical and health sciences medicine claudin Animals Caenorhabditis elegans Proteins Claudin Actin 030304 developmental biology General Immunology and Microbiology fungi Membrane Proteins biology.organism_classification Actins PVD Gene Expression Regulation Claudins 030217 neurology & neurosurgery Developmental Biology Neuroscience |
| Zdroj: | eLife, Vol 8 (2019) eLife |
| DOI: | 10.1101/347567 |
| Popis: | SummaryDevelopment of dendritic arbors is crucial for nervous system assembly, but the intracellular mechanisms that govern these processes remain incompletely understood. Here we show that the complex dendritic trees of PVD somatosensory neurons inCaenorhabditis elegansare patterned by distinct pathways downstream of the DMA-1 leucine rich transmembrane (LRR-TM) receptor. The guanine nucleotide exchange factortiam-1/GEFandact-4/Actinfunction with the DMA-1/LRR-TM to pattern 4° higher order branches by localizing F-actin to the distal ends of developing dendrites. Biochemical experiments show that DMA-1/LRR-TM is part of a biochemical complex with TIAM-1/GEF and ACT-4/Actin. Surprisingly, TIAM-1/GEF appears to function independently of Rac1 guanine nucleotide exchange factor activity. Additionally, another pathway dependent on HPO-30/Claudin and TIAM-1/GEF is required for formation of 2° and 3° branches. Collectively, our experiments suggest that the DMA-1/LRR-TM receptor on PVD dendrites may control aspects of dendrite patterning by directly modulating F-actin dynamics, independently of TIAM-1/GEF enzymatic activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|