Crystal structure of PRY‐SPRY domain of human TRIM72

Park, Eun Young; Kwon, Oh Bong; Jeong, Byung Cheon; Yi, Jae Sung; Lee, Chang Seok; Ko, Young Gyu; Song, Hyun Kyu

doi:10.1002/prot.22647

Cited by 40 publications

(42 citation statements)

References 31 publications

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“…However, the biochemical features of molecules that bind to TRIM72 have not been explicitly determined through in vitro binding experiments. To date, in vitro analyses have been carried out using only water-soluble constructs such as tagged TRIM72 proteins or deletion mutants (2,8). In the current study, the binding properties of untagged/undeleted and intact TRIM72 were evaluated.…”

Section: Discussionmentioning

confidence: 99%

“…Using domain homology analysis, TRIM72 was shown to have a variety of functional activities (7). TRIM72 consists of a RING finger domain, a B-box, two coiled coil domains, and a spla and ryanodine receptor (SPRY) domain (8). Among those functional domains, the B-box domain and two coiled coil domains are known to be molecular interacting domains (8).…”

Section: Introductionmentioning

confidence: 99%

“…TRIM72 consists of a RING finger domain, a B-box, two coiled coil domains, and a spla and ryanodine receptor (SPRY) domain (8). Among those functional domains, the B-box domain and two coiled coil domains are known to be molecular interacting domains (8). Recently, the structure of the PRY-SPRY domain of TRIM72 was determined by X-ray crystallography (8).…”

Section: Introductionmentioning

confidence: 99%

“…Among those functional domains, the B-box domain and two coiled coil domains are known to be molecular interacting domains (8). Recently, the structure of the PRY-SPRY domain of TRIM72 was determined by X-ray crystallography (8). From the crystal structure, it was suggested that the PRY-SPRY domain may be responsible for the protein-protein interaction (8).…”

Section: Introductionmentioning

confidence: 99%

“…Recently, the structure of the PRY-SPRY domain of TRIM72 was determined by X-ray crystallography (8). From the crystal structure, it was suggested that the PRY-SPRY domain may be responsible for the protein-protein interaction (8). However, no binding partner to TRIM72 has been identified.…”

Section: Introductionmentioning

confidence: 99%

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Lipid-binding properties of TRIM72

Kim¹,

Seo²,

Ko³

et al. 2012

BMB Reports

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TRIM72 is known to play a critical role in skeletal muscle membrane repair. To better understand the molecular mechanisms of this protein, we carried out an in vitro binding study with TRIM72. Our study proved that TRIM72 binds various lipids with dissociation constants (Kd) ranging from 88.2 ± 9.9 nM to 550.5 ± 134.5 nM. In addition, the intrinsic fluorescence of TRIM72 exponentially decreased when the protein was diluted with stirring. The time-resolved fluorescence decay occurred in a concentration-independent manner. The fluorescence-decayed TRIM72 remained in its secondary structure, but its binding properties were significantly reduced. The dissociation constants (Kd) of fluorescence-decayed TRIM72 for palmitate and stearate were 159.1 ± 39.9 nM and 355.4 ± 106.0 nM, respectively. This study suggests that TRIM72 can be dynamically converted by various stimuli. The results of this study also provide insight into the role of TRIM72 in the repair of sarcolemma damage. (BMB reports 2012; 45(1): 26-31)

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Lipid-binding properties of TRIM72

Kim¹,

Seo²,

Ko³

et al. 2012

BMB Reports

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A MID1 gene mutation in a patient with Opitz G/BBB syndrome that altered the 3D structure of SPRY domain

Liu

et al. 2012

American J of Med Genetics Pt A

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Mutations in the MID1 gene result in X-linked Opitz G/BBB syndrome (OS), a disorder that affects development of midline structures and comprises hypertelorism, cleft lip/palate, hypospadias, and laryngo-tracheo-esophageal abnormalities, and, at times, neurological, anal, and cardiac defects. MID1 gene abnormalities include missense, nonsense, and splicing mutations, small insertions, small deletions, and complex rearrangements. Here, we present a patient with Opitz G/BBB syndrome and a unique MID1 gene point mutation c.1703T

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TRIM72 contributes to cardiac fibrosis via regulating STAT3/Notch‐1 signaling

Feng

et al. 2019

Journal Cellular Physiology

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Cardiac fibrosis is a pathophysiological process characterized by excessive deposition of extracellular matrix. We developed a cardiac hypertrophy model using transverse aortic constriction (TAC) to uncover mechanisms relevant to excessive deposition of extracellular matrix in mouse myocardial cells. TAC caused upregulation of Tripartite motif protein 72 (TRIM72), a tripartite motif‐containing protein that is critical for proliferation and migration. Importantly, in vivo silencing of TRIM72 reversed TAC‐induced cardiac fibrosis, as indicated by markedly increased left ventricular systolic pressure and decreased left ventricular end‐diastolic pressure. TRIM72 knockdown also attenuated deposition of fibrosis marker collagen type I and α‐smooth muscle actin (α‐SMA). In an in vitro study, TRIM72 was similarly upregulated in cardiac fibroblasts. Knockdown of TRIM72 markedly suppressed collagen type I and α‐SMA expression and significantly decreased the proliferation and migration of cardiac fibroblasts. However, TRIM72 overexpression markedly increased collagen type I and α‐SMA expression and increased the proliferation and migration of cardiac fibroblasts. Further study demonstrated that TRIM72 increased phosphorylated STAT3 in cardiac fibroblasts. TRIM72 knockdown in cardiac fibroblasts resulted in increased expression of Notch ligand Jagged‐1 and its downstream gene and Notch‐1 intracellular domain. Inhibition of Notch‐1 abrogated sh‐TRIM72‐induced cardiac fibrosis. Together, our results support a novel role for TRIM72 in maintaining fibroblast‐to‐myofibroblast transition and suppressing fibroblast growth by regulating the STAT3/Notch‐1 pathway.

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Crystal structure of PRY‐SPRY domain of human TRIM72

Cited by 40 publications

References 31 publications

Lipid-binding properties of TRIM72

Lipid-binding properties of TRIM72

A MID1 gene mutation in a patient with Opitz G/BBB syndrome that altered the 3D structure of SPRY domain

TRIM72 contributes to cardiac fibrosis via regulating STAT3/Notch‐1 signaling

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