scholarly journals Author response: A high-resolution morphological and ultrastructural map of anterior sensory cilia and glia in Caenorhabditis elegans

2014 ◽  
Author(s):  
David B Doroquez ◽  
Cristina Berciu ◽  
James R Anderson ◽  
Piali Sengupta ◽  
Daniela Nicastro
Keyword(s):  
Caenorhabditis Elegans ◽  
High Resolution ◽  
Author Response ◽  
Sensory Cilia

scholarly journals Author response: The insulin/IGF signaling cascade modulates SUMOylation to regulate aging and proteostasis in Caenorhabditis elegans

2018 ◽  
Author(s):  
Lorna Moll ◽  
Noa Roitenberg ◽  
Michal Bejerano-Sagie ◽  
Hana Boocholez ◽  
Filipa Carvalhal Marques ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Author Response ◽  
Signaling Cascade ◽  
Igf Signaling

scholarly journals Genetic or Toxicant-Induced Disruption of Vesicular Monoamine Storage and Global Metabolic Profiling in Caenorhabditis elegans

2021 ◽  
Author(s):  
Joshua M Bradner ◽  
Vrinda Kalia ◽  
Fion K Lau ◽  
Monica Sharma ◽  
Meghan L Bucher ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Caenorhabditis Elegans ◽  
High Resolution ◽  
High Resolution Mass Spectrometry ◽  
Dopamine Neurons ◽  
Vesicular Monoamine Transporter ◽  
Monoamine Transporter ◽  
C Elegans ◽  
High Resolution Mass ◽  
Resolution Mass

Abstract The proper storage and release of monoamines contributes to a wide range of neuronal activity. Here, we examine the effects of altered vesicular monoamine transport in the nematode Caenorhabditis elegans. The gene cat-1 is responsible for the encoding of the vesicular monoamine transporter (VMAT) in C. elegans and is analogous to the mammalian vesicular monoamine transporter 2 (VMAT2). Our laboratory has previously shown that reduced VMAT2 activity confers vulnerability on catecholamine neurons in mice. The purpose of this article was to determine whether this function is conserved and to determine the impact of reduced VMAT activity in C. elegans. Here we show that deletion of cat-1/VMAT increases sensitivity to the neurotoxicant 1-methyl-4-phenylpyridinium (MPP+) as measured by enhanced degeneration of dopamine neurons. Reduced cat-1/VMAT also induces changes in dopamine-mediated behaviors. High-resolution mass spectrometry-based metabolomics in the whole organism reveals changes in amino acid metabolism, including tyrosine metabolism in the cat-1/VMAT mutants. Treatment with MPP+ disrupted tryptophan metabolism. Both conditions altered glycerophospholipid metabolism, suggesting a convergent pathway of neuronal dysfunction. Our results demonstrate the evolutionarily conserved nature of monoamine function in C. elegans and further suggest that high-resolution mass spectrometry-based metabolomics can be used in this model to study environmental and genetic contributors to complex human disease.

Author response for "Determination of Tautomeric Preference of Fenobam in Solution by High Resolution NMR Spectroscopy"

2020 ◽  
Author(s):  
Xuming Sha ◽  
Shaodong Chen ◽  
Xiaojing Zheng ◽  
Xin Ye ◽  
Hailu Zhang ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
High Resolution ◽  
Author Response ◽  
High Resolution Nmr

scholarly journals Automated cellular annotation for high-resolution images of adult Caenorhabditis elegans

2013 ◽  
Vol 29 (13) ◽  
pp. i18-i26 ◽  
Author(s):  
S. J. Aerni ◽  
X. Liu ◽  
C. B. Do ◽  
S. S. Gross ◽  
A. Nguyen ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
High Resolution ◽  
High Resolution Images

scholarly journals Caenorhabditis elegans DYF-2, an Orthologue of Human WDR19, Is a Component of the Intraflagellar Transport Machinery in Sensory Cilia

2006 ◽  
Vol 17 (11) ◽  
pp. 4801-4811 ◽  
Author(s):  
Evgeni Efimenko ◽  
Oliver E. Blacque ◽  
Guangshuo Ou ◽  
Courtney J. Haycraft ◽  
Bradley K. Yoder ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Aspartic Acid ◽  
Critical Role ◽  
Intraflagellar Transport ◽  
Bardet Biedl Syndrome ◽  
Evolutionarily Conserved ◽  
Sensory Cilia ◽  
Mutant Phenotypes ◽  
And Function

The intraflagellar transport (IFT) machinery required to build functional cilia consists of a multisubunit complex whose molecular composition, organization, and function are poorly understood. Here, we describe a novel tryptophan-aspartic acid (WD) repeat (WDR) containing IFT protein from Caenorhabditis elegans, DYF-2, that plays a critical role in maintaining the structural and functional integrity of the IFT machinery. We determined the identity of the dyf-2 gene by transgenic rescue of mutant phenotypes and by sequencing of mutant alleles. Loss of DYF-2 function selectively affects the assembly and motility of different IFT components and leads to defects in cilia structure and chemosensation in the nematode. Based on these observations, and the analysis of DYF-2 movement in a Bardet–Biedl syndrome mutant with partially disrupted IFT particles, we conclude that DYF-2 can associate with IFT particle complex B. At the same time, mutations in dyf-2 can interfere with the function of complex A components, suggesting an important role of this protein in the assembly of the IFT particle as a whole. Importantly, the mouse orthologue of DYF-2, WDR19, also localizes to cilia, pointing to an important evolutionarily conserved role for this WDR protein in cilia development and function.

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