Related Experiment Video

Updated: May 17, 2026

Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion
09:23

Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion

Published on: April 2, 2020

RSK2 protein suppresses integrin activation and fibronectin matrix assembly and promotes cell migration

Joanna E Gawecka1, Shirley S Young-Robbins, Florian J Sulzmaier

  • 1Cancer Biology Program, University of Hawaii Cancer Center, Honolulu, Hawaii 96813, USA.

The Journal of Biological Chemistry
|November 3, 2012
PubMed

Insights

Ribosomal S6 Kinase 2 (RSK2) regulates integrin activation, impairing cell adhesion and matrix assembly while promoting motility and cancer metastasis. RSK2 acts as a key mediator in this process.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Integrin activation is crucial for cell adhesion, migration, and extracellular matrix assembly.
  • Ribosomal S6 Kinase 2 (RSK2) is known to promote tumor cell motility and metastasis downstream of Ras/Raf signaling.

Purpose of the Study:

  • To investigate the role of RSK2 in regulating integrin function.
  • To elucidate the mechanism by which RSK2 influences cell behavior relevant to cancer metastasis.

Main Methods:

  • Investigated RSK2's effect on integrin activation and associated cellular functions.
  • Examined RSK2 localization, co-localization with talin, and effects on actin stress fibers and focal adhesions.
  • Assessed filamin phosphorylation and binding to integrins upon RSK2 activation.
  • Studied RSK2 activation in response to integrin ligation.

Main Results:

  • RSK2 mediates Ras/Raf-induced inactivation of integrins.
  • RSK2 impairs cell adhesion, integrin-mediated matrix assembly, and promotes cell motility.
  • RSK2 reduces actin stress fibers, disrupts focal adhesions, and co-localizes with talin at integrin tails.
  • RSK2 activation promotes filamin phosphorylation and binding to integrins, and is itself activated by integrin ligation.

Conclusions:

  • RSK2 is a key regulator of integrin activity, influencing cell adhesion, migration, and matrix assembly.
  • RSK2's mechanism involves modulating integrin activation, potentially through talin interaction and filamin phosphorylation.
  • RSK2 may participate in a feedback loop controlling integrin function and promoting cancer metastasis.

More Related Videos

Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration10:43

Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration

Published on: May 19, 2016

Vasodilation of Isolated Vessels and the Isolation of the Extracellular Matrix of Tight-skin Mice08:09

Vasodilation of Isolated Vessels and the Isolation of the Extracellular Matrix of Tight-skin Mice

Published on: March 24, 2017

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...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Cytoskeletal Coordination in Cell Migration01:32

Cytoskeletal Coordination in Cell Migration

A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker proteins that...
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II  is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction. It is...