Related Experiment Video

Updated: May 23, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

The extracellular signal-regulated kinase 3 (mitogen-activated protein kinase 6 [MAPK6])-MAPK-activated protein

Frank Brand1, Stefanie Schumacher, Shashi Kant

  • 1Institute of Physiological Chemistry, Hannover Medical School, Hannover, Germany.

Molecular and Cellular Biology
|April 18, 2012
PubMed

Insights

Mitogen-activated protein kinase-activated protein kinase 5 (MK5) deficiency impairs neuronal development. The ERK3/MK5 signaling module regulates dendrite and spine formation by interacting with Septin7.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Mitogen-activated protein kinase-activated protein kinase 5 (MAPKAP) kinase 5 (MK5) deficiency is linked to reduced extracellular signal-regulated kinase 3 (ERK3) levels.
  • Understanding the physiological roles of the ERK3/MK5 signaling module is crucial for neuroscience research.

Purpose of the Study:

  • To investigate the physiological functions of the ERK3/MK5 signaling module in neuronal development.
  • To identify novel interacting partners and substrates within the ERK3/MK5 pathway.

Main Methods:

  • Utilized a mitogen-activated protein kinase-activated protein kinase 5 (MK5) knockout mouse model.
  • Performed large-scale interaction screens to identify protein partners.
  • Analyzed dendritic spine formation in mouse hippocampal neurons in vivo and in transfected primary neurons.

Main Results:

  • MK5-deficient mice exhibited impaired dendritic spine formation.
  • Septin7 (Sept7) was identified as a novel interacting partner of ERK3, forming a ternary complex with ERK3/MK5.
  • The ERK3/MK5 module phosphorylates Sept7 regulators (Binders of Rho GTPases - Borgs) and interacts with kalirin-7 (Kal7).
  • Sept7-dependent dendrite development and spine formation are stimulated by the ERK3/MK5 module.

Conclusions:

  • The ERK3/MK5 signaling module plays a critical role in regulating neuronal morphogenesis.
  • This study proposes neuronal morphogenesis as the first identified physiological function of the ERK3/MK5 signaling module.

More Related Videos

Using Drosophila Larval Neuromuscular Junction and Muscle Cells to Visualize Microtubule Network08:04

Using Drosophila Larval Neuromuscular Junction and Muscle Cells to Visualize Microtubule Network

Published on: October 20, 2023

Genetic Manipulation of Cerebellar Granule Neurons In Vitro and In Vivo to Study Neuronal Morphology and Migration09:07

Genetic Manipulation of Cerebellar Granule Neurons In Vitro and In Vivo to Study Neuronal Morphology and Migration

Published on: March 17, 2014

Related Concept Videos

MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
Role of Septins01:02

Role of Septins

Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
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...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Septins01:19

Septins

Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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,...