Ignet

Gene Information

Gene symbol: SDK1

Gene name: sidekick cell adhesion molecule 1

HGNC ID: 19307

Synonyms: FLJ31425

Related Genes

#	Gene Symbol	Number of hits
1	ACTN4	1 hits
2	CTNNB1	1 hits
3	MAGI1	1 hits
4	NPHS1	1 hits
5	SDK2	1 hits
6	SYNPO	1 hits

Related Sentences

#	PMID	Sentence
1	15213259	Sdk-1 and its ortholog, sidekick-2 (sdk-2), were recently shown to guide axonal terminals to specific synapses in developing neurons.
2	15213259	The current study demonstrates developmental expression of both sdk-1 and sdk-2 and a tight spatial and temporal regulation of these genes in kidney.
3	15213259	Sdk-1 and its ortholog, sidekick-2 (sdk-2), were recently shown to guide axonal terminals to specific synapses in developing neurons.
4	15213259	The current study demonstrates developmental expression of both sdk-1 and sdk-2 and a tight spatial and temporal regulation of these genes in kidney.
5	15703275	Sidekick-1 and its ortholog sidekick-2 have also been shown to function as neuronal targeting molecules, guiding developing neurons to specific synapses.
6	15703275	Furthermore, cells transfected with a chimeric sidekick, where the first two Ig domains of sidekick-2 are replaced with the corresponding two Ig domains of sidekick-1, form aggregates with sidekick-1-transfected cells.
7	15703275	The reverse chimera, where the first two Ig domains of sidekick-2 are substituted onto sidekick-1, was similarly able to form aggregates with sidekick-2-transfected cells.
8	15703275	Sidekick-1 and its ortholog sidekick-2 have also been shown to function as neuronal targeting molecules, guiding developing neurons to specific synapses.
9	15703275	Furthermore, cells transfected with a chimeric sidekick, where the first two Ig domains of sidekick-2 are replaced with the corresponding two Ig domains of sidekick-1, form aggregates with sidekick-1-transfected cells.
10	15703275	The reverse chimera, where the first two Ig domains of sidekick-2 are substituted onto sidekick-1, was similarly able to form aggregates with sidekick-2-transfected cells.
11	15703275	Sidekick-1 and its ortholog sidekick-2 have also been shown to function as neuronal targeting molecules, guiding developing neurons to specific synapses.
12	15703275	Furthermore, cells transfected with a chimeric sidekick, where the first two Ig domains of sidekick-2 are replaced with the corresponding two Ig domains of sidekick-1, form aggregates with sidekick-1-transfected cells.
13	15703275	The reverse chimera, where the first two Ig domains of sidekick-2 are substituted onto sidekick-1, was similarly able to form aggregates with sidekick-2-transfected cells.
14	20562105	In the current work, we demonstrate that the homophilic adhesion molecule sidekick-1 (sdk-1) is up-regulated in podocytes in FSGS both in rodent models and in human kidney biopsy samples.
15	20562105	Transgenic mice that have podocyte-specific overexpression of sdk-1 develop gradually progressive heavy proteinuria and severe FSGS.
16	20562105	We also show that sdk-1 associates with the slit diaphragm linker protein MAGI-1, which is already known to interact with several critical podocyte proteins including synaptopodin, alpha-actinin-4, nephrin, JAM4, and beta-catenin.
17	20562105	This interaction is mediated through a direct interaction between the carboxyl terminus of sdk-1 and specific PDZ domains of MAGI-1.
18	20562105	In vitro expression of sdk-1 enables a dramatic recruitment of MAGI-1 to the cell membrane.
19	20562105	Furthermore, a truncated version of sdk-1 that is unable to bind to MAGI-1 does not induce podocyte dysfunction when overexpressed.
20	20562105	We conclude that the up-regulation of sdk-1 in podocytes is an important pathogenic factor in FSGS and that the mechanism involves disruption of the actin cytoskeleton possibly via alterations in MAGI-1 function.
21	20562105	In the current work, we demonstrate that the homophilic adhesion molecule sidekick-1 (sdk-1) is up-regulated in podocytes in FSGS both in rodent models and in human kidney biopsy samples.
22	20562105	Transgenic mice that have podocyte-specific overexpression of sdk-1 develop gradually progressive heavy proteinuria and severe FSGS.
23	20562105	We also show that sdk-1 associates with the slit diaphragm linker protein MAGI-1, which is already known to interact with several critical podocyte proteins including synaptopodin, alpha-actinin-4, nephrin, JAM4, and beta-catenin.
24	20562105	This interaction is mediated through a direct interaction between the carboxyl terminus of sdk-1 and specific PDZ domains of MAGI-1.
25	20562105	In vitro expression of sdk-1 enables a dramatic recruitment of MAGI-1 to the cell membrane.
26	20562105	Furthermore, a truncated version of sdk-1 that is unable to bind to MAGI-1 does not induce podocyte dysfunction when overexpressed.
27	20562105	We conclude that the up-regulation of sdk-1 in podocytes is an important pathogenic factor in FSGS and that the mechanism involves disruption of the actin cytoskeleton possibly via alterations in MAGI-1 function.
28	20562105	In the current work, we demonstrate that the homophilic adhesion molecule sidekick-1 (sdk-1) is up-regulated in podocytes in FSGS both in rodent models and in human kidney biopsy samples.
29	20562105	Transgenic mice that have podocyte-specific overexpression of sdk-1 develop gradually progressive heavy proteinuria and severe FSGS.
30	20562105	We also show that sdk-1 associates with the slit diaphragm linker protein MAGI-1, which is already known to interact with several critical podocyte proteins including synaptopodin, alpha-actinin-4, nephrin, JAM4, and beta-catenin.
31	20562105	This interaction is mediated through a direct interaction between the carboxyl terminus of sdk-1 and specific PDZ domains of MAGI-1.
32	20562105	In vitro expression of sdk-1 enables a dramatic recruitment of MAGI-1 to the cell membrane.
33	20562105	Furthermore, a truncated version of sdk-1 that is unable to bind to MAGI-1 does not induce podocyte dysfunction when overexpressed.
34	20562105	We conclude that the up-regulation of sdk-1 in podocytes is an important pathogenic factor in FSGS and that the mechanism involves disruption of the actin cytoskeleton possibly via alterations in MAGI-1 function.
35	20562105	In the current work, we demonstrate that the homophilic adhesion molecule sidekick-1 (sdk-1) is up-regulated in podocytes in FSGS both in rodent models and in human kidney biopsy samples.
36	20562105	Transgenic mice that have podocyte-specific overexpression of sdk-1 develop gradually progressive heavy proteinuria and severe FSGS.
37	20562105	We also show that sdk-1 associates with the slit diaphragm linker protein MAGI-1, which is already known to interact with several critical podocyte proteins including synaptopodin, alpha-actinin-4, nephrin, JAM4, and beta-catenin.
38	20562105	This interaction is mediated through a direct interaction between the carboxyl terminus of sdk-1 and specific PDZ domains of MAGI-1.
39	20562105	In vitro expression of sdk-1 enables a dramatic recruitment of MAGI-1 to the cell membrane.
40	20562105	Furthermore, a truncated version of sdk-1 that is unable to bind to MAGI-1 does not induce podocyte dysfunction when overexpressed.
41	20562105	We conclude that the up-regulation of sdk-1 in podocytes is an important pathogenic factor in FSGS and that the mechanism involves disruption of the actin cytoskeleton possibly via alterations in MAGI-1 function.
42	20562105	In the current work, we demonstrate that the homophilic adhesion molecule sidekick-1 (sdk-1) is up-regulated in podocytes in FSGS both in rodent models and in human kidney biopsy samples.
43	20562105	Transgenic mice that have podocyte-specific overexpression of sdk-1 develop gradually progressive heavy proteinuria and severe FSGS.
44	20562105	We also show that sdk-1 associates with the slit diaphragm linker protein MAGI-1, which is already known to interact with several critical podocyte proteins including synaptopodin, alpha-actinin-4, nephrin, JAM4, and beta-catenin.
45	20562105	This interaction is mediated through a direct interaction between the carboxyl terminus of sdk-1 and specific PDZ domains of MAGI-1.
46	20562105	In vitro expression of sdk-1 enables a dramatic recruitment of MAGI-1 to the cell membrane.
47	20562105	Furthermore, a truncated version of sdk-1 that is unable to bind to MAGI-1 does not induce podocyte dysfunction when overexpressed.
48	20562105	We conclude that the up-regulation of sdk-1 in podocytes is an important pathogenic factor in FSGS and that the mechanism involves disruption of the actin cytoskeleton possibly via alterations in MAGI-1 function.
49	20562105	In the current work, we demonstrate that the homophilic adhesion molecule sidekick-1 (sdk-1) is up-regulated in podocytes in FSGS both in rodent models and in human kidney biopsy samples.
50	20562105	Transgenic mice that have podocyte-specific overexpression of sdk-1 develop gradually progressive heavy proteinuria and severe FSGS.
51	20562105	We also show that sdk-1 associates with the slit diaphragm linker protein MAGI-1, which is already known to interact with several critical podocyte proteins including synaptopodin, alpha-actinin-4, nephrin, JAM4, and beta-catenin.
52	20562105	This interaction is mediated through a direct interaction between the carboxyl terminus of sdk-1 and specific PDZ domains of MAGI-1.
53	20562105	In vitro expression of sdk-1 enables a dramatic recruitment of MAGI-1 to the cell membrane.
54	20562105	Furthermore, a truncated version of sdk-1 that is unable to bind to MAGI-1 does not induce podocyte dysfunction when overexpressed.
55	20562105	We conclude that the up-regulation of sdk-1 in podocytes is an important pathogenic factor in FSGS and that the mechanism involves disruption of the actin cytoskeleton possibly via alterations in MAGI-1 function.
56	20562105	In the current work, we demonstrate that the homophilic adhesion molecule sidekick-1 (sdk-1) is up-regulated in podocytes in FSGS both in rodent models and in human kidney biopsy samples.
57	20562105	Transgenic mice that have podocyte-specific overexpression of sdk-1 develop gradually progressive heavy proteinuria and severe FSGS.
58	20562105	We also show that sdk-1 associates with the slit diaphragm linker protein MAGI-1, which is already known to interact with several critical podocyte proteins including synaptopodin, alpha-actinin-4, nephrin, JAM4, and beta-catenin.
59	20562105	This interaction is mediated through a direct interaction between the carboxyl terminus of sdk-1 and specific PDZ domains of MAGI-1.
60	20562105	In vitro expression of sdk-1 enables a dramatic recruitment of MAGI-1 to the cell membrane.
61	20562105	Furthermore, a truncated version of sdk-1 that is unable to bind to MAGI-1 does not induce podocyte dysfunction when overexpressed.
62	20562105	We conclude that the up-regulation of sdk-1 in podocytes is an important pathogenic factor in FSGS and that the mechanism involves disruption of the actin cytoskeleton possibly via alterations in MAGI-1 function.