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Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
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Homer binds a novel proline rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors
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Tu J.C., Xiao B., Yuan J., Lanahan A., Leoffert K., Li M., Linden D., Worley P.F. Homer binds a novel proline rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors. Neuron. 21:1998;717-726. Homer proteins are demonstrated to couple mGluRs with IP3 receptors in a signaling complex. The immediate early gene form of Homer protein (Homer 1a) is shown to regulate coupling efficiency, thereby defining a synaptic function for Homer 1a proteins.
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Ciruela F., Soloviev M.M., Chan W.Y., McIlhinney R.A. Homer-1c/Vesl-1L modulates the cell surface targeting of metabotropic glutamate receptor type 1α: evidence for an anchoring function. Mol Cell Neurosci. 15:2000;36-50.
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Presents an initial report of the effect of Homer on mGluR trafficking. CC-Homers cause the retention of group 1 mGluRs in the ER, whereas Homer 1a is permissive for insertion of the mature receptor into the plasma membrane. The action of CC-Homer requires direct protein-protein interaction with the receptor. Extensive pools of ER-associated mGluRs are demonstrated in CNS neurons, suggesting that Homer may play a similar 'receptor trafficking' role in in vivo systems.
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Roche K.W., Tu J.C., Petralia R.S., Xiao B., Wenthold R.J., Worley P.F. Homer 1b regulates the trafficking of group I metabotropic glutamate receptors. J Biol Chem. 274:1999;25953-25957. Presents an initial report of the effect of Homer on mGluR trafficking. CC-Homers cause the retention of group 1 mGluRs in the ER, whereas Homer 1a is permissive for insertion of the mature receptor into the plasma membrane. The action of CC-Homer requires direct protein-protein interaction with the receptor. Extensive pools of ER-associated mGluRs are demonstrated in CNS neurons, suggesting that Homer may play a similar 'receptor trafficking' role in in vivo systems.
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Vesl, a gene encoding VASP/Ena family related protein, is upregulated during seizure, long-term potentiation and synaptogenesis
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Describes the extended family of Homer/Vesl proteins. New members of the Homer/Vesl family are demonstrated to encode coiled-coil (CC) domains and self-associate. Because the IEG form (Homer 1a) lacks a CC domain, it was suggested that it functions as a natural dominant negative.
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Kato A., Ozawa F., Saitoh Y., Fukazawa Y., Sugiyama H., Inokuchi K. Novel members of the Vesl/Homer family of PDZ proteins that bind metabotropic glutamate receptors. J Biol Chem. 273:1998;23969-23975. Describes the extended family of Homer/Vesl proteins. New members of the Homer/Vesl family are demonstrated to encode coiled-coil (CC) domains and self-associate. Because the IEG form (Homer 1a) lacks a CC domain, it was suggested that it functions as a natural dominant negative.
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Kato, A.1
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Homer regulates the association of group 1 metabotropic receptors with multivalent complexes of Homer-related, synaptic proteins
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Describes the extended family of Homer/Vesl proteins and the current Homer nomenclature. CC-Homer proteins are visualized at the PSD and are demonstrated to self associate in vivo. Transgenic mice that overexpress Homer 1a demonstrate its ability to regulate the coupling of CC-Homer to group 1 mGluRs.
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Xiao B., Tu J.C., Petralia R.S., Yuan J., Doan A., Breder C., Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F. Homer regulates the association of group 1 metabotropic receptors with multivalent complexes of Homer-related, synaptic proteins. Neuron. 21:1998;707-716. Describes the extended family of Homer/Vesl proteins and the current Homer nomenclature. CC-Homer proteins are visualized at the PSD and are demonstrated to self associate in vivo. Transgenic mice that overexpress Homer 1a demonstrate its ability to regulate the coupling of CC-Homer to group 1 mGluRs.
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Xiao, B.1
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Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition
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Presents the structure of the Homer EVH1 domain, which elucidates the distinctive binding properties of the Homer subfamily. Mena/VASP EVH1 domains bind FPPPP, whereas Homer EVH1 binds PPXXF. The orientation of the peptides as they are bound to their respective EVH1 domains is identical, and binding specificity is conferred by distinct pockets for the phenylalanine.
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Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition. Neuron. 26:2000;143-154. Presents the structure of the Homer EVH1 domain, which elucidates the distinctive binding properties of the Homer subfamily. Mena/VASP EVH1 domains bind FPPPP, whereas Homer EVH1 binds PPXXF. The orientation of the peptides as they are bound to their respective EVH1 domains is identical, and binding specificity is conferred by distinct pockets for the phenylalanine.
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The self-association properties of the Homer CC domain are examined and shown to be mediated by several different domains. This article anticipates the complexity of CC-Homer self-multimerization.
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Tadokoro S., Tachibana T., Imanaka T., Nishida W., Sobue K. Involvement of unique leucine-zipper motif of PSD-Zip45 (Homer 1c/vesl-1L) in group 1 metabotropic glutamate receptor clustering. Proc Natl Acad Sci USA. 96:1999;13801-13806. The self-association properties of the Homer CC domain are examined and shown to be mediated by several different domains. This article anticipates the complexity of CC-Homer self-multimerization.
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19
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Cupidin, an isoform of Homer/Vesl, interacts with the actin cytoskeleton and activated rho family small GTPases and is expressed in developing mouse cerebellar granule cells
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Reports the association of the amino terminus of Cupidin (Homer 2a) with F-actin and an association of its carboxy-terminal domain with Cdc42. If confirmed in natural systems, the interactions of Homer proteins with cytoskeletal elements suggests functions for Homer in addition to those detailed in the present review.
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Shiraishi Y., Mizutani A., Bito H., Fujisawa K., Narumiya S., Mikoshiba K., Furuichi T. Cupidin, an isoform of Homer/Vesl, interacts with the actin cytoskeleton and activated rho family small GTPases and is expressed in developing mouse cerebellar granule cells. J Neurosci. 19:1999;8389-8400. Reports the association of the amino terminus of Cupidin (Homer 2a) with F-actin and an association of its carboxy-terminal domain with Cdc42. If confirmed in natural systems, the interactions of Homer proteins with cytoskeletal elements suggests functions for Homer in addition to those detailed in the present review.
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Describes multiple Homer cDNAs, including Homer 2 EVH1-only transcipts. This report suggests that additional dominant-negative forms of Homer may be generated and function in peripheral tissues.
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