Related Experiment Video

Updated: Apr 19, 2026

Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans
08:47

Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans

Published on: July 5, 2019

10.6K

MTM-6, a phosphoinositide phosphatase, is required to promote synapse formation in Caenorhabditis elegans

Vivian R Ericson1, Kerri A Spilker1, Madina S Tugizova1

  • 1Department of Biology, Howard Hughes Medical Institute, Stanford University, Stanford, California, United States of America.

Plos One
|December 6, 2014
PubMed

Insights

Loss of the phosphoinositide phosphatase MTM-6 reduces synaptic connections by affecting Wnt ligand EGL-20 secretion and neuronal activity. This study reveals a novel neuronal role for MTM-6 in synaptic development.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Proper synapse formation is essential for neuronal development and function.
  • Synaptic density is regulated by complex molecular signaling pathways, including Wnt signaling.
  • Phosphoinositide phosphatases play critical roles in cellular processes, but their specific roles in synaptic development are not fully understood.

Purpose of the Study:

  • To investigate the function of the phosphoinositide phosphatase mtm-6 in neuronal development.
  • To determine the role of MTM-6 in regulating synapse formation and synaptic puncta number.
  • To elucidate the molecular mechanisms by which MTM-6 influences synaptic development, particularly its interaction with Wnt signaling.

Main Methods:

  • Utilized genetic loss-of-function studies in model organisms to assess the impact on synaptic puncta.
  • Investigated the regulation of Wnt ligand secretion, specifically EGL-20, by MTM-6.
  • Examined the specificity of MTM-6 activity towards different Wnt ligands.
  • Analyzed the expression pattern of MTM-6 in relation to its function.

Main Results:

  • Loss of mtm-6 function leads to a significant reduction in the number of synaptic puncta.
  • This reduction in synapses is partly due to MTM-6's regulation of EGL-20 secretion from tail cells.
  • MTM-6 exhibits relative specificity for regulating EGL-20 secretion compared to other Wnt ligands.
  • A novel neuronal function for MTM-6 was identified.

Conclusions:

  • MTM-6 is crucial for proper synapse formation during neuronal development.
  • MTM-6 regulates synaptic development through both Wnt ligand secretion and direct neuronal action.
  • The regulation of Wnt ligand secretion can involve distinct molecular components, highlighting pathway specificity.
  • MTM-6 possesses a previously unrecognized role in neuronal function.

More Related Videos

Determining Genetic Expression Profiles in C. elegans Using Microarray and Real-time PCR10:27

Determining Genetic Expression Profiles in C. elegans Using Microarray and Real-time PCR

Published on: July 30, 2011

23.9K
In vivo Assessment of Microtubule Dynamics and Orientation in Caenorhabditis elegans Neurons07:43

In vivo Assessment of Microtubule Dynamics and Orientation in Caenorhabditis elegans Neurons

Published on: November 20, 2021

3.7K

Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
7.2K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.1K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
6.4K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.8K