TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of ElK-1 and AP-1

Wang, Yuequn; Li, Yongqing; Qi, Xinzhu; Yuan, Wuzhou; Ai, Jianping; Zhu, Chuanbing; Cao, Lei; Yang, Hong; Liu, Fang; Wu, Xiushan; Liu, Mingyao

doi:10.1016/j.bbrc.2004.08.048

Cited by 52 publications

(29 citation statements)

References 32 publications

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“…The TRIM family of proteins is large and displays diverse cell biological functions (12,30). Previous studies have linked TRIM protein function to several human diseases, including muscular dystrophy, viral infection, and cancer progression (9).…”

Section: Discussionmentioning

confidence: 99%

MG53 Regulates Membrane Budding and Exocytosis in Muscle Cells

Cai

Masumiya

Weisleder

et al. 2009

Journal of Biological Chemistry

104

134

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Membrane recycling and remodeling contribute to multiple cellular functions, including cell fusion events during myogenesis. We have identified a tripartite motif (TRIM72) family member protein named MG53 and defined its role in mediating the dynamic process of membrane fusion and exocytosis in striated muscle. MG53 is a muscle-specific protein that contains a TRIM motif at the amino terminus and a SPRY motif at the carboxyl terminus. Live cell imaging of green fluorescent protein-MG53 fusion construct in cultured myoblasts showed that although MG53 contains no transmembrane segment it is tightly associated with intracellular vesicles and sarcolemmal membrane. RNA interference-mediated knockdown of MG53 expression impeded myoblast differentiation, whereas overexpression of MG53 enhanced vesicle trafficking to and budding from sarcolemmal membrane. Co-expression studies indicated that MG53 activity is regulated by a functional interaction with caveolin-3. Our data reveal a new function for TRIM family proteins in regulating membrane trafficking and fusion in striated muscles.When myoblasts exit the cell cycle during myogenesis, dramatic changes in membrane organization occur as myoblast fusion allows the formation of multinucleated muscle fibers. In addition to cell fusion events, differentiation of myotubes involves establishment of specialized membrane structures (1, 2). The transverse tubular invagination of sarcolemmal membrane and the intracellular membrane network known as the sarcoplasmic reticulum are two highly organized membrane architectures in cardiac and skeletal muscle. Establishment of these intricate membrane compartments requires extensive remodeling of the immature myoblast membranes. Dynamic membrane remodeling also contributes to many physiologic processes in mature muscle, including Ca 2ϩ signaling, trafficking of glucose transporter (GLUT4), and other membrane internalization events involving caveolae structures (3-6). Although defects in membrane integrity have been linked to various forms of muscular dystrophy (7,8), the molecular machinery regulating these specific membrane recycling and remodeling events in striated muscle is not well defined.The large tripartite motif (TRIM) 5 family of proteins is involved in numerous cellular functions in a wide variety of cell types. Members of this protein family contain signature motifs that include a RING finger, a zinc binding moiety (B-box), and a coiled coil structure (RBCC), which invariably comprise the amino-terminal domain of TRIM family members (9). The carboxyl-terminal sequence of TRIM proteins is variable; in some cases a subfamily of TRIM proteins contains a SPRY domain, a sequence first observed in the ryanodine receptor Ca 2ϩ channel in the sarcoplasmic reticulum membrane of excitable cells (10). Extensive studies have revealed that protein-protein interactions in the cytosol mediate the defined functions of TRIM proteins. For example, the ubiquitin E3 ligase enzymatic activity of several TRIM family members requires the B-box motif ...

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Section: Discussionmentioning

confidence: 99%

MG53 Regulates Membrane Budding and Exocytosis in Muscle Cells

Cai

Masumiya

Weisleder

et al. 2009

Journal of Biological Chemistry

104

134

View full text Add to dashboard Cite

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“…It has been reported that TRIM45 is expressed in the nucleus and cytoplasm in COS-7 cells [23]. Next, we performed immunofluorescence staining to confirm the subcellular localization of TRIM45 using COS-7 cells.…”

Section: Trim45 Is Predominantly Localized In the Perinuclear Regionmentioning

confidence: 94%

“…It has been reported that TRIM45 is expressed in various human tissues including the skeletal muscle, brain, heart, and pancreas [23]. We amplified human TRIM45…”

Section: Expression Of Human and Mouse Trim45 In Mammalian Cellsmentioning

confidence: 99%

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TRIM45 negatively regulates NF-κB-mediated transcription and suppresses cell proliferation

Shibata¹,

Satô²,

Nukiwa³

et al. 2012

Biochemical and Biophysical Research Communications

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1 These two individuals contributed equally to this work. Key words: TRIM45, NF-B, MAPK, TNF , cell proliferation 2 AbstractThe NF-B signaling pathway plays an important role in cell survival, immunity, inflammation, carcinogenesis, and organogenesis. Activation of NF-B is regulated by several posttranslational modifications including phosphorylation, neddylation and ubiquitination. The NF-B signaling pathway is activated by two distinct signaling mechanisms and is strictly modulated by the ubiquitin-proteasome system. It has been reported that overexpression of TRIM45, one of the TRIM family ubiquitin ligases, suppresses transcriptional activities of Elk-1 and AP-1, which are targets of the MAPK signaling pathway. In this study, we showed that TRIM45 also negatively regulates TNF -induced NF-B-mediated transcription by a luciferase reporter assay and that TRIM45 lacking a RING domain also has an activity to inhibit the NF-B signal.Moreover, we found that TRIM45 overexpression suppresses cell growth. These findings suggest that TRIM45 acts as a repressor for the NF-B signal and regulates cell growth.3

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“…The 80 days embryo multiple tissue membrane were hybridized with cDNA probe of ZNF 424 and β-actin cDNA probe (Clontech). The method of Northern blot was described in previous studies (24).…”

Section: Rna Isolation and Northern Blot Hybridizationmentioning

confidence: 99%

TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of ElK-1 and AP-1

Cited by 52 publications

References 32 publications

MG53 Regulates Membrane Budding and Exocytosis in Muscle Cells

MG53 Regulates Membrane Budding and Exocytosis in Muscle Cells

TRIM45 negatively regulates NF-κB-mediated transcription and suppresses cell proliferation

ZNF424, a novel human KRAB/C2H2 zinc finger protein, suppresses NFAT and p21 pathway

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