Integrin-actin interactions

Wiesner, Sebastian; Legate, Kyle R.; Fässler, Reinhard

doi:10.1007/s00018-005-4522-8

Cited by 170 publications

(120 citation statements)

References 266 publications

Supporting

Mentioning

117

Contrasting

Unclassified

Order By: Relevance

“…S5) (10). Integrins drive changes in cell shape by affecting the actin cytoskeleton (21). Accordingly, we found that internal perfusion of the actin polymerizing inhibitor latrunculin A (latA, 0.1 M) delivered through the patch pipette eliminated MMP-9-induced spine expansion and synaptic potentiation (Fig.…”

Section: Resultsmentioning

confidence: 82%

Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately

Wang

Bozdagi

Nikitczuk

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

293

323

View full text Add to dashboard Cite

Persistent dendritic spine enlargement is associated with stable long-term potentiation (LTP), and the latter is thought to underlie long-lasting memories. Extracellular proteolytic remodeling of the synaptic microenvironment could be important for such plasticity, but whether or how proteolytic remodeling contributes to persistent modifications in synapse structure and function is unknown. Matrix metalloproteinase-9 (MMP-9) is an extracellular protease that is activated perisynaptically after LTP induction and required for LTP maintenance. Here, by monitoring spine size and excitatory postsynaptic potentials (EPSPs) simultaneously with combined 2-photon time-lapse imaging and whole-cell recordings from hippocampal neurons, we find that MMP-9 is both necessary and sufficient to drive spine enlargement and synaptic potentiation concomitantly. Both structural and functional MMP-driven forms of plasticity are mediated through ␤1-containing integrin receptors, are associated with integrin-dependent cofilin inactivation within spines, and require actin polymerization. In contrast, postsynaptic exocytosis and protein synthesis are both required for MMP-9-induced potentiation, but not for initial MMP-9-induced spine expansion. However, spine expansion becomes unstable when postsynaptic exocytosis or protein synthesis is blocked, indicating that the 2 forms of plasticity are expressed independently but require interactions between them for persistence. When MMP activity is eliminated during theta-stimulation-induced LTP, both spine enlargement and synaptic potentiation are transient. Thus, MMP-mediated extracellular remodeling during LTP has an instructive role in establishing persistent modifications in both synapse structure and function of the kind critical for learning and memory.actin ͉ cofilin ͉ integrin ͉ synaptic plasticity ͉ protein synthesis L ong-lasting memory is based on long-term modifications of synapse structure and function. In hippocampal area CA1, naturalistic patterns of theta-stimulation readily induce long-term potentiation (LTP) of the excitatory, glutamatergic Schaffer collateral afferent inputs that target dendritic spines (1), which are small, actin-rich dendritic protrusions that harbor the majority of the excitatory synapses (2). Studies show that dendritic spines undergo significant morphological remodeling in association with long-lasting plasticity (3). Spine growth, for example, is associated with the induction of LTP and is thought to be important for supporting persistent changes in synaptic strength (4-6). However, little is known about signals that instruct and coordinate persistent modifications in synapse structure and function during LTP.Dendritic spine morphology and synaptic potentiation can both be dynamically modulated by proteins of the extracellular matrix (ECM) and the cell-surface proteins with which they interact, which has long fueled the idea that regulated ECM remodeling has an important role in synaptic plasticity (7). How precisely such remodeling could occur is not u...

show abstract

Section: Resultsmentioning

confidence: 82%

Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately

Wang

Bozdagi

Nikitczuk

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

293

323

View full text Add to dashboard Cite

show abstract

“…5 The direct partner of CAP1 is likely to be Talin because CAP1 interacts with Talin in yeast two-hybrid screens. 37 Talin is a cytoskeletal protein that is also a component of focal adhesion complexes, 38 providing a physical link between integrins and the cytoskeleton by binding to the cytoplasmic portion of integrin. During cell adhesion, it induces conformational changes in integrin extracellular domains that result in increased affinity for ligands.…”

Section: Cap1 Depletion Likely Activates Integrin Pathway Through Insmentioning

confidence: 99%

Mammalian CAP (Cyclase-associated protein) in the world of cell migration

Zhou

Zhang

Field

2013

Cell Adhesion & Migration

View full text Add to dashboard Cite

“…These proteins have been shown to have a central role in modulating integrin-dependent cell behaviors, including cell adhesion, migration and spreading. 54 Aberrant Rho GTPases signalling has, therefore, a profound impact on various aspects of cancer pathophysiology. Importantly, CD151 overexpression was found to activate Rac, Cdc42, but not Rho in A431 epidermoid carcinoma cells.…”

Section: Modulation Of Integrin-ligand Interactionsmentioning

confidence: 99%

CD151 in cancer progression and metastasis: a complex scenario

Sądej

Grudowska

Turczyk

et al. 2014

Laboratory Investigation

View full text Add to dashboard Cite

Originally identified as a molecular organizer of interacting proteins into tetraspanin-enriched microdomains, the tetraspanin CD151 has now been shown to be involved in tumour progression. Increasing evidence emerging from in vitro, in vivo and clinical analyses implicates this tetraspanin in supporting growth of various types of tumours at different levels. It affects both cell autonomous behavior and communication with neighboring cells and the microenvironment. CD151 regulates post-adhesion events, that is, cell spreading, migration and invasion including subsequent intravasation and formation of metastasis. Present on both neoplastic and endothelial cells, CD151 is engaged in promotion of tumour neovascularization. The molecular mechanism of CD151 in cancer is based on its ability to organize distribution and function of interacting proteins, ie, laminin-binding integrins (a3b1, a6b1 and a6b4), receptors for growth factors (HGFR, EGFR and TGF-b1R) and matrix metalloproteinases (MMP-7, MMP-2 and MMP-9), which indicates its importance in disease development. Results of clinical analyses of CD151 expression in different types of cancer and a large number of in vivo models demonstrate its impact on tumour growth and invasion and implicate CD151 as a valuable diagnostic and prognostic marker as well as a potential target for anti-cancer therapy. INTRODUCTIONTumour cells progress through multiple orchestrated steps before metastatic lesions are established in distant organs. These steps include detachment from the primary tumour mass, invasion of the basement membrane, migration through the surrounding extracellular matrix (ECM) followed by intravasation and extravasation and, finally, colonization of a secondary anatomical site. Successful completion of this sequence requires intrinsic changes enabling phenotypic transformation of the cell and, at every step, its coordinated communication with the tumour's microenvironment. A complex network of intricate tumourstroma interactions involves integrin-dependent adhesion and cell migration on the ECM, ECM degradation by matrix metalloproteinases (MMPs), and activation of signalling pathways responsible for cell survival, proliferation and motility, triggered by growth factor receptors stimulated by the environment.

show abstract

Integrin-actin interactions

Cited by 170 publications

References 266 publications

Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately

Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately

Mammalian CAP (Cyclase-associated protein) in the world of cell migration

CD151 in cancer progression and metastasis: a complex scenario

Contact Info

Product

Resources

About