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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Differentiation
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Cell Line
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Cell Proliferation
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Cerebellum / cytology
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Cerebellum / metabolism
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Cytoskeletal Proteins
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Gene Expression Regulation
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Glucosidases / genetics
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Glucosidases / metabolism*
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Humans
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Intracellular Signaling Peptides and Proteins / genetics
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Intracellular Signaling Peptides and Proteins / metabolism*
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Intracellular Signaling Peptides and Proteins / physiology*
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Mice
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism
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Nerve Tissue Proteins / physiology*
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Neurites / metabolism
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Neurites / physiology*
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Organ Specificity
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Protein Binding
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Protein Interaction Domains and Motifs
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Proteoglycans / metabolism
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Proteolysis*
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Tripartite Motif Proteins
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Two-Hybrid System Techniques
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Ubiquitination
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Vesicular Transport Proteins / metabolism
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ras Proteins / metabolism*
Substances
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Cytoskeletal Proteins
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Intracellular Signaling Peptides and Proteins
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Nerve Tissue Proteins
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Prkcsh protein, mouse
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Proteoglycans
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TRIM67 protein, mouse
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Tripartite Motif Proteins
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Vesicular Transport Proteins
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serglycin
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Glucosidases
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ras Proteins