The Experts below are selected from a list of 5442 Experts worldwide ranked by ideXlab platform
Eunjoon Kim - One of the best experts on this subject based on the ideXlab platform.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and beta PIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of beta PIX. Shank colocalizes with beta PIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with beta PIX and beta PIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of beta PIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits beta PIX and PAK to spines for the regulation of Postsynaptic Structure.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and βPIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of βPIX. Shank colocalizes with βPIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with βPIX and βPIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of βPIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits βPIX and PAK to spines for the regulation of Postsynaptic Structure.
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regulation of dendritic spine morphology by spar a psd 95 associated rapgap
Neuron, 2001Co-Authors: Daniel T S Pak, Soyoung Yang, Sheila Rudolphcorreia, Eunjoon Kim, Morgan ShengAbstract:The PSD-95/SAP90 family of scaffold proteins organizes the Postsynaptic density (PSD) and regulates NMDA receptor signaling at excitatory synapses. We report that SPAR, a Rap-specific GTPase-activating protein (RapGAP), interacts with the guanylate kinase-like domain of PSD-95 and forms a complex with PSD-95 and NMDA receptors in brain. In heterologous cells, SPAR reorganizes the actin cytoskeleton and recruits PSD-95 to F-actin. In hippocampal neurons, SPAR localizes to dendritic spines and causes enlargement of spine heads, many of which adopt an irregular appearance with putative multiple synapses. Dominant negative SPAR constructs cause narrowing and elongation of spines. The effects of SPAR on spine morphology depend on the RapGAP and actin-interacting domains, implicating Rap signaling in the regulation of Postsynaptic Structure.
Morgan Sheng - One of the best experts on this subject based on the ideXlab platform.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and beta PIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of beta PIX. Shank colocalizes with beta PIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with beta PIX and beta PIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of beta PIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits beta PIX and PAK to spines for the regulation of Postsynaptic Structure.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and βPIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of βPIX. Shank colocalizes with βPIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with βPIX and βPIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of βPIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits βPIX and PAK to spines for the regulation of Postsynaptic Structure.
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regulation of dendritic spine morphology by spar a psd 95 associated rapgap
Neuron, 2001Co-Authors: Daniel T S Pak, Soyoung Yang, Sheila Rudolphcorreia, Eunjoon Kim, Morgan ShengAbstract:The PSD-95/SAP90 family of scaffold proteins organizes the Postsynaptic density (PSD) and regulates NMDA receptor signaling at excitatory synapses. We report that SPAR, a Rap-specific GTPase-activating protein (RapGAP), interacts with the guanylate kinase-like domain of PSD-95 and forms a complex with PSD-95 and NMDA receptors in brain. In heterologous cells, SPAR reorganizes the actin cytoskeleton and recruits PSD-95 to F-actin. In hippocampal neurons, SPAR localizes to dendritic spines and causes enlargement of spine heads, many of which adopt an irregular appearance with putative multiple synapses. Dominant negative SPAR constructs cause narrowing and elongation of spines. The effects of SPAR on spine morphology depend on the RapGAP and actin-interacting domains, implicating Rap signaling in the regulation of Postsynaptic Structure.
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yotiao a novel protein of neuromuscular junction and brain that interacts with specific splice variants of nmda receptor subunit nr1
The Journal of Neuroscience, 1998Co-Authors: Michael Wyszynski, Raghavan Madhavan, Robert Sealock, Morgan ShengAbstract:The molecular machinery underlying neurotransmitter receptor immobilization at Postsynaptic sites is poorly understood. The NMDA receptor subunit NR1 can form clusters in heterologous cells via a mechanism dependent on the alternatively spliced C1 exon cassette in its intracellular C-terminal tail, suggesting a functional interaction between NR1 and the cytoskeleton. The yeast two-hybrid screen was used here to identify yotiao, a novel coiled coil protein that interacts with NR1 in a C1 exon-dependent manner. Yotiao mRNA (11 kb) is present modestly in brain and abundantly in skeletal muscle and pancreas. On Western blots, yotiao appears as an ∼230 kDa band that is present in cerebral cortex, hippocampus, and cerebellum. Biochemical studies reveal that yotiao fractionates with cytoskeleton-associated proteins and with the Postsynaptic density. With regard to immunohistochemistry, two anti-yotiao antibodies display a somatodendritic staining pattern similar to each other and to the staining pattern of NR1. Yotiao was colocalized by double-label immunocytochemistry with NR1 in rat brain and could be coimmunoprecipitated with NR1 from heterologous cells. Thus yotiao is an NR1-binding protein potentially involved in cytoskeletal attachment of NMDA receptors. Consistent with a general involvement in Postsynaptic Structure, yotiao was also found to be specifically concentrated at the neuromuscular junction in skeletal muscle.
Eunhye Park - One of the best experts on this subject based on the ideXlab platform.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and βPIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of βPIX. Shank colocalizes with βPIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with βPIX and βPIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of βPIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits βPIX and PAK to spines for the regulation of Postsynaptic Structure.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and beta PIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of beta PIX. Shank colocalizes with beta PIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with beta PIX and beta PIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of beta PIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits beta PIX and PAK to spines for the regulation of Postsynaptic Structure.
Jaeran Lee - One of the best experts on this subject based on the ideXlab platform.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and βPIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of βPIX. Shank colocalizes with βPIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with βPIX and βPIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of βPIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits βPIX and PAK to spines for the regulation of Postsynaptic Structure.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and beta PIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of beta PIX. Shank colocalizes with beta PIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with beta PIX and beta PIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of beta PIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits beta PIX and PAK to spines for the regulation of Postsynaptic Structure.
Seho Kim - One of the best experts on this subject based on the ideXlab platform.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and βPIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of βPIX. Shank colocalizes with βPIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with βPIX and βPIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of βPIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits βPIX and PAK to spines for the regulation of Postsynaptic Structure.
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the shank family of Postsynaptic density proteins interacts with and promotes synaptic accumulation of the βpix guanine nucleotide exchange factor for rac1 and cdc42
Journal of Biological Chemistry, 2003Co-Authors: Eunhye Park, Morgan Sheng, Jeonghoon Choi, Seho Kim, Jaeran Lee, Jiyoung Yoon, Dongeun Park, Eunjoon KimAbstract:The Shank/ProSAP family of multidomain proteins is known to play an important role in organizing synaptic multiprotein complexes. Here we report a novel interaction between Shank and beta PIX, a guanine nucleotide exchange factor for the Rac1 and Cdc42 small GTPases. This interaction is mediated by the PDZ domain of Shank and the C-terminal leucine zipper domain and the PDZ domain-binding motif at the extreme C terminus of beta PIX. Shank colocalizes with beta PIX at excitatory synaptic sites in cultured neurons. In brain, Shank forms a complex with beta PIX and beta PIX-associated signaling molecules including p21-associated kinase (PAK), an effector kinase of Rac1/Cdc42. Importantly, overexpression of Shank in cultured neurons promotes synaptic accumulation of beta PIX and PAK. Considering the involvement of Rac1 and PAK in spine dynamics, these results suggest that Shank recruits beta PIX and PAK to spines for the regulation of Postsynaptic Structure.