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PMID:22337885

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Citation

Yaguchi, H, Okumura, F, Takahashi, H, Kano, T, Kameda, H, Uchigashima, M, Tanaka, S, Watanabe, M, Sasaki, H and Hatakeyama, S (2012) TRIM67 protein negatively regulates Ras activity through degradation of 80K-H and induces neuritogenesis. J. Biol. Chem. 287:12050-9

Abstract

Tripartite motif (TRIM)-containing proteins, which are defined by the presence of a common domain structure composed of a RING finger, one or two B-box motifs and a coiled-coil motif, are involved in many biological processes including innate immunity, viral infection, carcinogenesis, and development. Here we show that TRIM67, which has a TRIM motif, an FN3 domain and a SPRY domain, is highly expressed in the cerebellum and that TRIM67 interacts with PRG-1 and 80K-H, which is involved in the Ras-mediated signaling pathway. Ectopic expression of TRIM67 results in degradation of endogenous 80K-H and attenuation of cell proliferation and enhances neuritogenesis in the neuroblastoma cell line N1E-115. Furthermore, morphological and biological changes caused by knockdown of 80K-H are similar to those observed by overexpression of TRIM67. These findings suggest that TRIM67 regulates Ras signaling via degradation of 80K-H, leading to neural differentiation including neuritogenesis.

Links

PubMed PMC3320951 Online version:10.1074/jbc.M111.307678

Keywords

Animals; Cell Differentiation; Cell Line; Cell Proliferation; Cerebellum/cytology; Cerebellum/metabolism; Gene Expression Regulation; Glucosidases/genetics; Glucosidases/metabolism; Humans; Intracellular Signaling Peptides and Proteins/genetics; Intracellular Signaling Peptides and Proteins/metabolism; Intracellular Signaling Peptides and Proteins/physiology; Mice; Nerve Tissue Proteins/genetics; Nerve Tissue Proteins/metabolism; Nerve Tissue Proteins/physiology; Neurites/metabolism; Neurites/physiology; Organ Specificity; Protein Binding; Protein Interaction Domains and Motifs; Proteoglycans/metabolism; Proteolysis; Two-Hybrid System Techniques; Ubiquitination; Vesicular Transport Proteins/metabolism; ras Proteins/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MOUSE:GLU2B

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

PR:Q505D9
PR:Q7TME0

F

Seeded From UniProt

complete

MOUSE:GLU2B

acts_upstream_of_or_within

GO:0010977: negative regulation of neuron projection development

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:TRI67

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

PR:O08795
PR:Q7TME0
PR:Q7TPB0

F

Seeded From UniProt

complete

MOUSE:TRI67

located_in

GO:0005737: cytoplasm

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

MOUSE:TRI67

acts_upstream_of_or_within

GO:0010976: positive regulation of neuron projection development

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:TRI67

acts_upstream_of_or_within

GO:0010976: positive regulation of neuron projection development

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:TRI67

acts_upstream_of_or_within

GO:0046580: negative regulation of Ras protein signal transduction

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:TRI67

acts_upstream_of_or_within

GO:2000060: positive regulation of ubiquitin-dependent protein catabolic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:PLPR4

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

PR:O08795
PR:Q7TME0

F

Seeded From UniProt

complete

MOUSE:PLPR3

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

PR:Q505D9
PR:Q7TME0

F

Seeded From UniProt

complete


See also

References

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