Membrane Localization of Membrane Type 5 Matrix Metalloproteinase by AMPA Receptor Binding Protein and Cleavage of Cadherins

Monea, Sara; Jordan, Bryen A.; Srivastava, Shalini; deSouza, Sunita; Ziff, Edward B.

doi:10.1523/jneurosci.3521-05.2006

Cited by 100 publications

(105 citation statements)

References 91 publications

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“…In addition, it has been previously shown that MT5-MMP activity generates a C-terminal fragment from Ncadherin cleavage in heterologous cells (20). Consistently, we have shown that N-cadherin is a substrate of MT5-MMP in vivo.…”

Section: Discussionsupporting

confidence: 89%

“…MT5-MMP can degrade several ECM components, such as inhibitory chondroitin sulfate proteoglycans, thereby promoting neurite outgrowth in vitro (16,19). Moreover, it appears capable of mediating the cleavage of cell-adhesion molecule N-cadherin in heterologous cells (20). On this basis, together with the absence of A␤-fiber sprouting after sciatic nerve injury in a mouse strain lacking MT5-MMP, it has been suggested that this metalloproteinase may contribute to the ECM degradation associated with neuronal plasticity (21).…”

Section: Peripheral Interactions Between Nociceptive Fibers and Mast mentioning

confidence: 99%

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Metalloproteinase MT5-MMP is an essential modulator of neuro-immune interactions in thermal pain stimulation

Folgueras

Valdés-Sánchez²,

Llano³

et al. 2009

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

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Peripheral interactions between nociceptive fibers and mast cells contribute to inflammatory pain, but little is known about mechanisms mediating neuro-immune communication. Here we show that metalloproteinase MT5-MMP (MMP-24) is an essential mediator of peripheral thermal nociception and inflammatory hyperalgesia. We report that MT5-MMP is expressed by CGRP-containing peptidergic nociceptors in dorsal root ganglia and that Mmp24-deficient mice display enhanced sensitivity to noxious thermal stimuli under basal conditions. Consistently, mutant peptidergic sensory neurons hyperinnervate the skin, a phenotype that correlates with changes in the regulated cleavage of the cell-cell adhesion molecule N-cadherin. In contrast to basal nociception, Mmp24 ؊/؊ mice do not develop thermal hyperalgesia during inflammation, a phenotype that appears associated with alterations in N-cadherin-mediated cell-cell interactions between mast cells and sensory fibers. Collectively, our findings demonstrate an essential role of MT5-MMP in the development of dermal neuro-immune synapses and suggest that this metalloproteinase may be a target for pain control.inflammation ͉ mast cell ͉ N-cadherin

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Section: Discussionsupporting

confidence: 89%

Section: Peripheral Interactions Between Nociceptive Fibers and Mast mentioning

confidence: 99%

Metalloproteinase MT5-MMP is an essential modulator of neuro-immune interactions in thermal pain stimulation

Folgueras

Valdés-Sánchez²,

Llano³

et al. 2009

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

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“…MT5-MMP can degrade purified proteoglycans and gelatin substrates in vitro (Wang et al, 1999a) and can also relieve the inhibitory function of proteoglycans during axonal elongation on laminin-coated plates (Hayashita-Kinoh et al, 2001). Moreover, it appears capable of mediating the cleavage of cell-adhesion molecule N-cadherin in heterologous cells (Monea et al, 2006). MT5-MMP (MMP-24) is mainly expressed in neuronal cells of both central and peripheral nervous systems, although its presence has been also detected in inflammatory cells (Bar-Or et al, 2003;Hayashita-Kinoh et al, 2001;Jaworski, 2000;Llano et al, 1999;Pei, 1999a).…”

Section: Neoplastic Diseasesmentioning

confidence: 99%

“…More than one human MT5-MMP transcript may exist in the central nervous system (Monea et al, 2006;Ross and Fillmore, 2007).…”

Section: Neoplastic Diseasesmentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

209

212

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a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

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“…GRIP proteins and PICK1 interact with GluA2 at the same site, but are differentially regulated by PKC-dependent phosphorylation of GluA2 Ser880 (10)(11)(12). In addition to GluA2/3, GRIP1 and 2 binds various signaling and cytoskeletal proteins, including EphB receptor tyrosine kinase, ephrinB ligands, α-liprin scaffolding protein, proteoglycan NG2, Fras1 and 2, GRIP1-associated protein 1 (GRASP-1), kinesin-1/KIF5 microtubule motor protein and matrix metalloproteinase 5 (13)(14)(15)(16)(17)(18)(19). Thus, GRIP proteins may serve to organize macromolecular complexes, linking AMPA-Rs and other membrane proteins to the cytoskeleton and membrane trafficking and signal transduction pathways.…”

mentioning

confidence: 99%

GRIP1 and 2 regulate activity-dependent AMPA receptor recycling via exocyst complex interactions

Mao

Takamiya

Thomas

et al. 2010

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

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PSD-95/SAP90/DLG/ZO-1 (PDZ) domain-mediated protein-protein interactions play important roles in regulating AMPA receptor trafficking and neuronal plasticity. GRIP1 and GRIP2 are homologous multi-PDZ domain-containing proteins that bind to the Ctermini of AMPA-R GluA2 and GluA3 subunits. Previous attempts to determine the cellular roles of GRIP1 and GRIP2 in neurons have been complicated by nonspecific reagents, and by the embryonic lethality of conventional GRIP1 KO mice. To circumvent these issues we developed a conditional targeted deletion strategy to knock out GRIP1 in postnatal neurons derived from GRIP2 KO mice. Loss of GRIP1 and 2 did not affect normal AMPA-R steadystate trafficking and endocytosis, but strikingly impaired activitydependent AMPA-R recycling. This previously uncharacterized role for GRIP1 appears to be mediated by novel interactions with the cellular trafficking machinery via the exocyst protein complex. Indeed, disruption of GRIP1-exocyst binding caused a strikingly similar deficit in AMPA-R recycling. Together these findings reveal a previously unidentified role for AMPA-R-GRIP1-exocyst protein complexes in activity-dependent AMPA-R trafficking.A MPA receptors conduct the majority of fast excitatory synaptic transmission in the mammalian central nervous system. Dynamic regulation of AMPA-R trafficking in and out of synapses modulates the efficacy of synaptic transmission and is crucial for synaptic plasticity (1-3). One major molecular mechanism that governs AMPA-R trafficking is the regulated interaction of intracellular C-termini of AMPA-R subunits with PSD-95/SAP90, DLG/ ZO-1 (PDZ) domain-containing proteins (4-7). The type II PDZ motifs of GluA2 and GluA3 C-termini interact with several PDZ domain-containing proteins, including PICK1 (6, 7) and the homologous GRIP1 and GRIP2 proteins (GRIP2 is also called ABP for AMPA-R binding protein) (4,5,8,9). GRIP proteins and PICK1 interact with GluA2 at the same site, but are differentially regulated by PKC-dependent phosphorylation of GluA2 Ser880 (10-12). In addition to GluA2/3, GRIP1 and 2 binds various signaling and cytoskeletal proteins, including EphB receptor tyrosine kinase, ephrinB ligands, α-liprin scaffolding protein, proteoglycan NG2, Fras1 and 2, GRIP1-associated protein 1 (GRASP-1), kinesin-1/KIF5 microtubule motor protein and matrix metalloproteinase 5 (13-19). Thus, GRIP proteins may serve to organize macromolecular complexes, linking AMPA-Rs and other membrane proteins to the cytoskeleton and membrane trafficking and signal transduction pathways.GRIP-GluA2/3 interactions are implicated in regulating AMPA-R synaptic targeting. Overexpression of the GluA2 C terminus in neurons decreases the synaptic targeting of AMPA-Rs (4). Point mutants of GluA2 that are unable to bind GRIP proteins exhibit reduced synaptic accumulation (20). GRIP1's sixth PDZ domain interacts with the α-liprin family of proteins, and disrupting GRIP-α-liprin interactions inhibits AMPA-R surface expression and synaptic targeting (14). GRIP proteins also bind ...

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Membrane Localization of Membrane Type 5 Matrix Metalloproteinase by AMPA Receptor Binding Protein and Cleavage of Cadherins

Cited by 100 publications

References 91 publications

Metalloproteinase MT5-MMP is an essential modulator of neuro-immune interactions in thermal pain stimulation

Metalloproteinase MT5-MMP is an essential modulator of neuro-immune interactions in thermal pain stimulation

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

GRIP1 and 2 regulate activity-dependent AMPA receptor recycling via exocyst complex interactions

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