scholarly journals The MicroRNA mir-71 Inhibits Calcium Signaling by Targeting the TIR-1/Sarm1 Adaptor Protein to Control Stochastic L/R Neuronal Asymmetry in C. elegans

PLoS Genetics ◽  
2012 ◽  
Vol 8 (8) ◽  
pp. e1002864 ◽  
Author(s):  
Yi-Wen Hsieh ◽  
Chieh Chang ◽  
Chiou-Fen Chuang
Keyword(s):  
Calcium Signaling ◽  
Adaptor Protein ◽  
C Elegans ◽  
Neuronal Asymmetry

scholarly journals Microtubule-based localization of a synaptic calcium-signaling complex is required for left-right neuronal asymmetry in C. elegans

Development ◽  
2011 ◽  
Vol 138 (16) ◽  
pp. 3509-3518 ◽  
Author(s):  
Chieh Chang ◽  
Yi-Wen Hsieh ◽  
Bluma J. Lesch ◽  
Cornelia I. Bargmann ◽  
Chiou-Fen Chuang
Keyword(s):  
Calcium Signaling ◽  
C Elegans ◽  
Signaling Complex ◽  
Neuronal Asymmetry

scholarly journals Stochastic left–right neuronal asymmetry in Caenorhabditis elegans

2016 ◽  
Vol 371 (1710) ◽  
pp. 20150407 ◽  
Author(s):  
Amel Alqadah ◽  
Yi-Wen Hsieh ◽  
Rui Xiong ◽  
Chiou-Fen Chuang
Keyword(s):  
Caenorhabditis Elegans ◽  
Molecular Mechanisms ◽  
Neurological Diseases ◽  
Calcium Signalling ◽  
Model Organism ◽  
Brain Asymmetry ◽  
C Elegans ◽  
Left And Right ◽  
Left Right Asymmetry ◽  
Neuronal Asymmetry

Left–right asymmetry in the nervous system is observed across species. Defects in left–right cerebral asymmetry are linked to several neurological diseases, but the molecular mechanisms underlying brain asymmetry in vertebrates are still not very well understood. The Caenorhabditis elegans left and right amphid wing ‘C’ (AWC) olfactory neurons communicate through intercellular calcium signalling in a transient embryonic gap junction neural network to specify two asymmetric subtypes, AWC OFF (default) and AWC ON (induced), in a stochastic manner. Here, we highlight the molecular mechanisms that establish and maintain stochastic AWC asymmetry. As the components of the AWC asymmetry pathway are highly conserved, insights from the model organism C. elegans may provide a window onto how brain asymmetry develops in humans. This article is part of the themed issue ‘Provocative questions in left–right asymmetry’.

scholarly journals Autophagosomes fuse to phagosomes and facilitate the degradation of apoptotic cells in Caenorhabditis elegans

eLife ◽  
2022 ◽  
Vol 11 ◽  
Author(s):  
Omar Peña-Ramos ◽  
Lucia Chiao ◽  
Xianghua Liu ◽  
Xiaomeng Yu ◽  
Tianyou Yao ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Apoptotic Cell ◽  
Adaptor Protein ◽  
Small Gtpase ◽  
Apoptotic Cells ◽  
Phagosome Maturation ◽  
Double Membrane ◽  
C Elegans ◽  
Intracellular Organelles ◽  
Cellular Components

Autophagosomes are double-membrane intracellular vesicles that degrade protein aggregates, intracellular organelles, and other cellular components. During the development of the nematode Caenorhabditis elegans, many somatic and germ cells undergo apoptosis. These cells are engulfed and degraded by their neighboring cells. We discovered a novel role of autophagosomes in facilitating the degradation of apoptotic cells using a real-time imaging technique. Specifically, the double-membrane autophagosomes in engulfing cells are recruited to the surfaces of phagosomes containing apoptotic cells and subsequently fuse to phagosomes, allowing the inner vesicle to enter the phagosomal lumen. Mutants defective in the production of autophagosomes display significant defects in the degradation of apoptotic cells, demonstrating the importance of autophagosomes to this process. The signaling pathway led by the phagocytic receptor CED-1, the adaptor protein CED-6, and the large GTPase dynamin (DYN-1) promotes the recruitment of autophagosomes to phagosomes. Moreover, the subsequent fusion of autophagosomes with phagosomes requires the functions of the small GTPase RAB-7 and the HOPS complex components. Further observations suggest that autophagosomes provide apoptotic cell-degradation activities in addition to and in parallel of lysosomes. Our findings reveal that, unlike the single-membrane, LC3-associated phagocytosis (LAP) vesicles reported for mammalian phagocytes, the canonical double-membrane autophagosomes facilitate the clearance of C. elegans apoptotic cells. These findings add autophagosomes to the collection of intracellular organelles that contribute to phagosome maturation, identify novel crosstalk between the autophagy and phagosome maturation pathways, and discover the upstream signaling molecules that initiate this crosstalk.

scholarly journals Acentrosomal spindle assembly and stability in C. elegans oocytes requires a kinesin-12 non-motor microtubule interaction domain

2021 ◽  
Author(s):  
Ian Daniel Wolff ◽  
Jeremy Alden Hollis ◽  
Sarah Marie Wignall
Keyword(s):  
Adaptor Protein ◽  
Direct Interaction ◽  
Spindle Assembly ◽  
Meiotic Spindle ◽  
Interaction Domain ◽  
Microtubule Binding ◽  
C Elegans ◽  
Insight Into

During the meiotic divisions in oocytes, microtubules are sorted and organized by motor proteins to generate a bipolar spindle in the absence of centrosomes. In most organisms, kinesin-5 family members crosslink and slide microtubules to generate outward force that promotes acentrosomal spindle bipolarity. However, the mechanistic basis for how other kinesin families act on acentrosomal spindles has not been explored. We investigated this question in C. elegans oocytes, where kinesin-5 is not required to generate outward force. Instead, the kinesin-12 family motor KLP-18 performs this function. KLP-18 acts with adaptor protein MESP-1 (meiotic spindle 1) to sort microtubule minus ends to the periphery of a microtubule array, where they coalesce into spindle poles. If either of these proteins is depleted, outward sorting of microtubules is lost and minus ends converge to form a monoaster. Here we use a combination of in vitro biochemical assays and in vivo mutant analysis to provide insight into the mechanism by which these proteins collaborate to promote acentrosomal spindle assembly. We identify a microtubule binding site on the C-terminal stalk of KLP-18 and demonstrate that a direct interaction between the KLP-18 stalk and MESP-1 activates non-motor microtubule binding. We also provide evidence that this C-terminal domain is required for KLP-18 activity during spindle assembly and show that KLP-18 is continuously required to maintain spindle bipolarity. This study thus provides new insight into the construction and maintenance of the oocyte acentrosomal spindle as well as into kinesin-12 mechanism and regulation.

scholarly journals Intercellular calcium signaling in a gap junction-coupled cell network establishes asymmetric neuronal fates in C. elegans

Development ◽  
2012 ◽  
Vol 139 (22) ◽  
pp. 4191-4201 ◽  
Author(s):  
J. A. Schumacher ◽  
Y.-W. Hsieh ◽  
S. Chen ◽  
J. K. Pirri ◽  
M. J. Alkema ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
Gap Junction ◽  
C Elegans ◽  
Cell Network

scholarly journals Behavioral adaptation in C. elegans produced by antipsychotic drugs requires serotonin and is associated with calcium signaling and calcineurin inhibition

2009 ◽  
Vol 64 (3) ◽  
pp. 280-289 ◽  
Author(s):  
Dallas R. Donohoe ◽  
Raymond A. Jarvis ◽  
Kathrine Weeks ◽  
Eric J. Aamodt ◽  
Donard S. Dwyer
Keyword(s):  
Calcium Signaling ◽  
Antipsychotic Drugs ◽  
Behavioral Adaptation ◽  
C Elegans ◽  
Calcineurin Inhibition

scholarly journals C. elegans PAT-4/ILK Functions as an Adaptor Protein within Integrin Adhesion Complexes

2002 ◽  
Vol 12 (10) ◽  
pp. 787-797 ◽  
Author(s):  
A.Craig Mackinnon ◽  
Hiroshi Qadota ◽  
Kenneth R. Norman ◽  
Donald G. Moerman ◽  
Benjamin D. Williams
Keyword(s):  
Adaptor Protein ◽  
C Elegans
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