Characterization of MALS/Velis-1, -2, and -3: a Family of Mammalian LIN-7 Homologs Enriched at Brain Synapses in Association with the Postsynaptic Density-95/NMDA Receptor Postsynaptic Complex

Jo, Kiwon; Derin, Rachel; Li, Min; Bredt, David S.

doi:10.1523/jneurosci.19-11-04189.1999

Cited by 168 publications

(160 citation statements)

References 37 publications

(68 reference statements)

Supporting

Mentioning

148

Contrasting

Order By: Relevance

“…83,84 Postsynaptically MALS is known to bind to NMDA receptors and also involved in the transport of NMDA receptor vesicle along microtubules. 85,86 MALS, an essential component of neurotransmitter release, exists as a component of a large presynaptic complex in which liprin-a is also a part. The synaptic AMPA and NMDA receptors have complex roles in the NAc in cocaine relapse.…”

Section: Discussionmentioning

confidence: 99%

Cytosolic proteomic alterations in the nucleus accumbens of cocaine overdose victims

2006

View full text Add to dashboard Cite

Chronic cocaine use in humans and animal models is known to lead to pronounced alterations in neuronal function in the nucleus accumbens (NAc), a brain region associated with drug reinforcement. Two-dimensional gel electrophoresis was used to compare protein alterations in the NAc between cocaine overdose (COD) victims (n = 10) and controls (n = 10). Following image normalization, spots with significantly differential image intensities (P < 0.05) were identified, excised, trypsin digested and analyzed by matrix-assisted laser desorption ionization-time of flight-time of flight. A total of 1407 spots were found to be present in a minimum of five subjects per group and the intensity of 18 spots was found to be differentially abundant between the groups, leading to positive identification of 15 proteins by peptide mass fingerprinting (PMF). Of an additional 37 protein spots that were constitutively expressed, 32 proteins were positively identified by PMF. Increased proteins in COD included b-tubulin, liprin-a3 and neuronal enolase, whereas decreased proteins included parvalbumin, ATP synthase b-chain and peroxiredoxin 2. The present data provide a preliminary protein profile of COD, suggesting the involvement of novel proteins and pathways in the expression of this complex disease. Additional studies are warranted to further characterize alterations in the differentially regulated proteins. Understanding the coordinated involvement of multiple proteins in cocaine abuse provides insight into the molecular basis of the disease and offers new targets for pharmacotherapeutic intervention for drug abuse-related disorders.

show abstract

Section: Discussionmentioning

confidence: 99%

Cytosolic proteomic alterations in the nucleus accumbens of cocaine overdose victims

2006

View full text Add to dashboard Cite

show abstract

“…Subcellular fractions were prepared by differential centrifugation as described previously (Jo et al, 1999). Ten rat cerebella were homogenized in 15 ml of buffer I (0.32 M sucrose, 3 mM HEPES-Na, pH 7.4, 0.1 mg/ml PMSF).…”

Section: Methodsmentioning

confidence: 99%

New Transmembrane AMPA Receptor Regulatory Protein Isoform, γ-7, Differentially Regulates AMPA Receptors

Kato¹,

Zhou²,

Milstein³

et al. 2007

J. Neurosci.

128

168

View full text Add to dashboard Cite

AMPA-type glutamate receptors (GluRs) mediate most excitatory signaling in the brain and are composed of GluR principal subunits and transmembrane AMPA receptor regulatory protein (TARP) auxiliary subunits. Previous studies identified four mammalian TARPs, ␥-2 (or stargazin), ␥-3, ␥-4, and ␥-8, that control AMPA receptor trafficking, gating, and pharmacology. Here, we explore roles for the homologous ␥-5 and ␥-7 proteins, which were previously suggested not to serve as TARPs. Western blotting reveals high levels of ␥-5 and ␥-7 in the cerebellum, where ␥-7 is enriched in Purkinje neurons in the molecular layer and glomerular synapses in the granule cell layer. Immunoprecipitation proteomics shows that cerebellar ␥-7 avidly and selectively binds to AMPA receptor GluR subunits and also binds to the AMPA receptor clustering protein, postsynaptic density-95 (PSD-95). Furthermore, ␥-7 occurs together with PSD-95 and AMPA receptor subunits in purified postsynaptic densities. In heterologous cells, ␥-7 but not ␥-5 greatly enhances AMPA receptor glutamateevoked currents and modulates channel gating. In granule cells from stargazer mice, transfection of ␥-7 but not ␥-5 increases AMPA receptor-mediated currents. Compared with stargazin, ␥-7 differentially modulates AMPA receptor glutamate affinity and kainate efficacy. These studies define ␥-7 as a new member of the TARP family that can differentially influence AMPA receptors in cerebellar neurons.

show abstract

“…Introduction mLin-7/Veli/MALS is a mammalian homologue of LIN-7 of C. elegans (Butz et al, 1998;Irie et al, 1999;Jo et al, 1999). LIN-7 has genetically been shown to function to localize the LET-23 receptor tyrosine kinase to the basolateral membrane of vulval precursor cells (Simske et al, 1996).…”

mentioning

confidence: 99%

“…There are mammalian homologues of LIN-2 and LIN-10: mLin-2/CASK/ Camguk and mLin-10/X11/Mint1, respectively (Duclos et al, 1993;Hata et al, 1996;Dimitratos et al, 1997;Okamoto and SuÈ dhof, 1997). mLin-7 has three isoforms: mLin-7A, -7B, and -7C (Butz et al, 1998;Irie et al, 1999;Jo et al, 1999). Each isoform has a single PSD-95/DLG/ZO-1 (PDZ) domain, which is highly homologous to each other.…”

mentioning

confidence: 99%

“…mLin-7 interacts with mLin-2, which furthermore interacts with mLin-10, resulting in the formation of a heterotrimeric complex (Borg et al, 1998;Butz et al, 1998). Moreover, mLin-7 interacts with many other proteins, including PSD-95, type 2 NMDA receptors, BGT-1, Pals, b-catenin, and VAM-1 (Jo et al, 1999;Perego et al, 1999Perego et al, , 2000Kamberov et al, 2000;Tseng et al, 2001). We have previously shown that mLin-7 localizes at cell ± cell junctions including adherens junctions (AJs) in cultured Madin-Darby canine kidney (MDCK) cells, but it remains unknown how mLin-7 localizes at AJs (Irie et al, 1999).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Localization of mLin-7 at nectin-based cell–cell junctions

et al. 2002

View full text Add to dashboard Cite

In C. elegans, lin-7 as well as lin-2/lin-10 is involved in the proper localization of the LET-23 receptor tyrosine kinase that regulates vulval induction. The mammalian homologue, mLin-7, forms a ternary complex with the mammalian homologues of LIN-2 and LIN-10 and localizes at cell ± cell junctions in epithelial cells, but the mechanism of this localization of mLin-7 is unknown. Nectin is an immunoglobulin-like cell ± cell adhesion molecule that is involved in organization of adherens and tight junctions in epithelial cells. Nectin is indirectly associated with the cadherin ± catenin system and the actin cytoskeleton through afadin, an actin ®lament-binding protein. We showed here that mLin-7 localized at the nectin-based cell ± cell junctions. This localization of mLin-7 required the interaction of nectin with afadin, but not the cadherin ± catenin system or the actin cytoskeleton. mLin-7 did not directly interact with nectin or afadin. The results indicate that mLin-7 localizes at cell ± cell junctions through the nectin ± afadin system.

show abstract

Characterization of MALS/Velis-1, -2, and -3: a Family of Mammalian LIN-7 Homologs Enriched at Brain Synapses in Association with the Postsynaptic Density-95/NMDA Receptor Postsynaptic Complex

Cited by 168 publications

References 37 publications

Cytosolic proteomic alterations in the nucleus accumbens of cocaine overdose victims

Cytosolic proteomic alterations in the nucleus accumbens of cocaine overdose victims

New Transmembrane AMPA Receptor Regulatory Protein Isoform, γ-7, Differentially Regulates AMPA Receptors

Localization of mLin-7 at nectin-based cell–cell junctions

Contact Info

Product

Resources

About