TY - JOUR
T1 - TIAM-1/GEF can shape somatosensory dendrites independently of its GEF activity by regulating F-actin localization
AU - Tang, Leo T.H.
AU - Diaz-Balzac, Carlos A.
AU - Rahman, Maisha
AU - Ramirez-Suarez, Nelson J.
AU - Salzberg, Yehuda
AU - Lázaro-Peña, Maria I.
AU - Bülow, Hannes E.
N1 - Publisher Copyright:
© 2019, eLife Sciences Publications Ltd. All rights reserved.
PY - 2019
Y1 - 2019
N2 - Dendritic arbors are crucial for nervous system assembly, but the intracellular mechanisms that govern their assembly remain incompletely understood. Here, we show that the dendrites of PVD neurons in Caenorhabditis elegans are patterned by distinct pathways downstream of the DMA-1 leucine-rich transmembrane (LRR-TM) receptor. DMA-1/LRR-TM interacts through a PDZ ligand motif with the guanine nucleotide exchange factor TIAM-1/GEF in a complex with act-4/Actin to pattern higher order 4˚ dendrite branches by localizing F-actin to the distal ends of developing dendrites. Surprisingly, TIAM-1/GEF appears to function independently of Rac1 guanine nucleotide exchange factor activity. A partially redundant pathway, dependent on HPO-30/Claudin, regulates formation of 2˚ and 3˚ branches, possibly by regulating membrane localization and trafficking of DMA-1/LRR-TM. Collectively, our experiments suggest that HPO-30/ Claudin localizes the DMA-1/LRR-TM receptor on PVD dendrites, which in turn can control dendrite patterning by directly modulating F-actin dynamics through TIAM-1/GEF.
AB - Dendritic arbors are crucial for nervous system assembly, but the intracellular mechanisms that govern their assembly remain incompletely understood. Here, we show that the dendrites of PVD neurons in Caenorhabditis elegans are patterned by distinct pathways downstream of the DMA-1 leucine-rich transmembrane (LRR-TM) receptor. DMA-1/LRR-TM interacts through a PDZ ligand motif with the guanine nucleotide exchange factor TIAM-1/GEF in a complex with act-4/Actin to pattern higher order 4˚ dendrite branches by localizing F-actin to the distal ends of developing dendrites. Surprisingly, TIAM-1/GEF appears to function independently of Rac1 guanine nucleotide exchange factor activity. A partially redundant pathway, dependent on HPO-30/Claudin, regulates formation of 2˚ and 3˚ branches, possibly by regulating membrane localization and trafficking of DMA-1/LRR-TM. Collectively, our experiments suggest that HPO-30/ Claudin localizes the DMA-1/LRR-TM receptor on PVD dendrites, which in turn can control dendrite patterning by directly modulating F-actin dynamics through TIAM-1/GEF.
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U2 - 10.7554/eLife.38949
DO - 10.7554/eLife.38949
M3 - Article
C2 - 30694177
AN - SCOPUS:85061254670
SN - 2050-084X
VL - 8
JO - eLife
JF - eLife
M1 - e38949
ER -