Related Experiment Video

Updated: Aug 16, 2026

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment
07:55

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment

Published on: September 25, 2017

Subcellular localization of PMES-2 proteins regulated by their two cytoskeleton-associated domains

Kensuke Ninomiya1, Tetsuya Ishimoto, Takahisa Taguchi

  • 1Research Institute for Cell Engineering (RICE), National Institute of Advanced Industrial Science and Technology (AIST), 1-8-31 Midorigaoka, Ikeda, Osaka, 563-8577, Japan.

Cellular and Molecular Neurobiology
|September 1, 2005
PubMed

Insights

The protein PMES-2 interacts with dynein light chain-2 (DLC-2), influencing its localization and synaptic function. This interaction is crucial for cytoskeletal organization and neuronal signaling.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • PMES-2 protein mRNA is found in hippocampal neuron neurites.
  • PMES-2 is located in the postsynaptic density, suggesting a role in synaptic function.

Purpose of the Study:

  • To investigate protein-protein interactions of PMES-2.
  • To understand the functional implications of PMES-2 interactions.

Main Methods:

  • Yeast two-hybrid screening was employed to identify PMES-2 interacting proteins.
  • Immunofluorescence was used to observe the localization of PMES-2 and its mutants.

Main Results:

  • PMES-2 was found to interact with dynein light chain-2 (DLC-2) through its C-terminal 20 amino acids.
  • Exogenous PMES-2 localized to the cell periphery with F-actin, while a mutant lacking the DLC-binding site localized to the nucleus.
  • A motif in the N-terminus of PMES-2 was identified as responsible for its dual targeting.

Conclusions:

  • PMES-2 acts as a linker between motor complexes and the membrane skeleton.
  • DLC-1/2 inhibits the nuclear localization of PMES-2.
  • PMES-2 may regulate cytoskeletal architecture, protein transport, and synaptic signal transduction to the nucleus.

More Related Videos

Identification of Plasmodesmal Localization Sequences in Proteins In Planta08:07

Identification of Plasmodesmal Localization Sequences in Proteins In Planta

Published on: August 15, 2017

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation10:52

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation

Published on: January 6, 2016

Related Concept Videos

Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Desmosomes01:05

Desmosomes

The term desmosome derives from the Greek words "desmo" and "soma" meaning "adhesion bodies." This structure was first observed during the late 1800s and described as small, dense nodules in the epidermis. Desmosomes are button-like structures that help form an interlinked network of intermediate filaments across the cells. These junctions are  essential to hold cells together under mechanical stress and to maintain tissue integrity. Desmosomes are multi-protein complexes comprising desmosomal...
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...