Related Experiment Video

Updated: Jun 16, 2026

Proliferation and Differentiation of Murine Myeloid Precursor 32D/G-CSF-R Cells
10:21

Proliferation and Differentiation of Murine Myeloid Precursor 32D/G-CSF-R Cells

Published on: February 21, 2018

Myeloid translocation gene 16b is a dual A-kinase anchoring protein that interacts selectively with plexins in a

Sarah E Fiedler1, Robynn V Schillace, Crystal J Daniels

  • 1VA Medical Center and Department of Endocrinology, Oregon Health & Sciences University, Portland, OR 97239, USA.

FEBS Letters
|February 9, 2010
PubMed

Insights

Mammalian MTG16b acts as a dual A-kinase anchoring protein (AKAP), binding to specific plexins in immune cells. This interaction integrates cyclic adenosine monophosphate (cAMP) and semaphorin signaling pathways.

Area of Science:

  • Molecular Biology
  • Immunology
  • Cell Signaling

Background:

  • Nervy, a myeloid translocation gene (MTG) homologue, functions as an A-kinase anchoring protein (AKAP) in Drosophila, modulating plexin-mediated semaphorin signaling.
  • Mammalian MTG16b is an AKAP identified in immune cells, where plexin-mediated semaphorin signaling is crucial for immune responses.

Purpose of the Study:

  • To investigate the role of mammalian MTG16b as a dual AKAP capable of binding plexins.
  • To explore the selectivity and regulation of MTG16b-plexin interactions.

Main Methods:

  • Biochemical assays to assess binding interactions between MTG16b and various plexins.
  • Analysis of PKA-phosphorylation effects on MTG16b-plexin binding.

Main Results:

  • MTG16b demonstrated dual AKAP capabilities, binding to specific plexins (PlexinA1 and PlexinA3) but not others (PlexinB1).
  • PKA-phosphorylation was found to regulate these selective MTG16b-plexin interactions.

Conclusions:

  • MTG16b serves as a bridge between cyclic adenosine monophosphate (cAMP) and semaphorin signaling pathways in immune cells.
  • This interaction provides a potential mechanism for integrating these two critical signaling cascades within the immune system.

More Related Videos

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors08:45

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

MISSION LentiPlex Pooled shRNA Library Screening in Mammalian Cells09:12

MISSION LentiPlex Pooled shRNA Library Screening in Mammalian Cells

Published on: December 21, 2011

Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
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...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
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...
The Ras Gene02:38

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...