Dataset Information

Specific Isoforms of the Guanine-Nucleotide Exchange Factor dPix Couple Neuromuscular Synapse Growth to Muscle Growth.

ABSTRACT: Developmental growth requires coordination between the growth rates of individual tissues and organs. Here, we examine how Drosophila neuromuscular synapses grow to match the size of their target muscles. We show that changes in muscle growth driven by autonomous modulation of insulin receptor signaling produce corresponding changes in synapse size, with each muscle affecting only its presynaptic motor neuron branches. This scaling growth is mechanistically distinct from synaptic plasticity driven by neuronal activity and requires increased postsynaptic differentiation induced by insulin receptor signaling in muscle. We identify the guanine-nucleotide exchange factor dPix as an effector of insulin receptor signaling. Alternatively spliced dPix isoforms that contain a specific exon are necessary and sufficient for postsynaptic differentiation and scaling growth, and their mRNA levels are regulated by insulin receptor signaling. These findings define a mechanism by which the same signaling pathway promotes both autonomous muscle growth and non-autonomous synapse growth.

SUBMITTER: Ho CH

PROVIDER: S-EPMC7346284 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Specific Isoforms of the Guanine-Nucleotide Exchange Factor dPix Couple Neuromuscular Synapse Growth to Muscle Growth.

Ho Cheuk Hei CH Treisman Jessica E JE

Developmental cell 20200608 1

Developmental growth requires coordination between the growth rates of individual tissues and organs. Here, we examine how Drosophila neuromuscular synapses grow to match the size of their target muscles. We show that changes in muscle growth driven by autonomous modulation of insulin receptor signaling produce corresponding changes in synapse size, with each muscle affecting only its presynaptic motor neuron branches. This scaling growth is mechanistically distinct from synaptic plasticity driv ...[more]

PMID: 32516570

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Project description:Cellular and viral factors participate in the replication cycle of rotavirus. We report that the guanine nucleotide exchange factor GBF1, which activates the small GTPase Arf1 to induce COPI transport processes, is required for rotavirus replication since knocking down GBF1 expression by RNA interference or inhibiting its activity by treatment with brefeldin A (BFA) or Golgicide A (GCA) significantly reduces the yield of infectious viral progeny. This reduction in virus yield was related to a block in virus assembly, since in the presence of either BFA or GCA, the assembly of infectious mature triple-layered virions was significantly prevented and only double-layered particles were detected. We report that the catalytic activity of GBF1, but not the activation of Arf1, is essential for the assembly of the outer capsid of rotavirus. We show that both BFA and GCA, as well as interfering with the synthesis of GBF1, alter the electrophoretic mobility of glycoproteins VP7 and NSP4 and block the trimerization of the virus surface protein VP7, a step required for its incorporation into virus particles. Although a posttranslational modification of VP7 (other than glycosylation) could be related to the lack of trimerization, we found that NSP4 might also be involved in this process, since knocking down its expression reduces VP7 trimerization. In support, recombinant VP7 protein overexpressed in transfected cells formed trimers only when cotransfected with NSP4.IMPORTANCE Rotavirus, a member of the family Reoviridae, is the major cause of severe diarrhea in children and young animals worldwide. Despite significant advances in the characterization of the biology of this virus, the mechanisms involved in morphogenesis of the virus particle are still poorly understood. In this work, we show that the guanine nucleotide exchange factor GBF1, relevant for COPI/Arf1-mediated cellular vesicular transport, participates in the replication cycle of the virus, influencing the correct processing of viral glycoproteins VP7 and NSP4 and the assembly of the virus surface proteins VP7 and VP4.

Dataset Information

Specific Isoforms of the Guanine-Nucleotide Exchange Factor dPix Couple Neuromuscular Synapse Growth to Muscle Growth.

Publications

Specific Isoforms of the Guanine-Nucleotide Exchange Factor dPix Couple Neuromuscular Synapse Growth to Muscle Growth.

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