Scaffold protein enigma homolog 1 overcomes the repression of myogenesis activation by inhibitor of DNA binding 2

Nakatani, Miyuki; Ito, Jin‐ichi; Koyama, Riko; Iijima, Masumi; Yoshimoto, Nobuo; Niimi, Tomoaki; Kuroda, Shinya; Maturana, Andrés D.

doi:10.1016/j.bbrc.2016.04.119

Cited by 7 publications

(7 citation statements)

References 35 publications

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“…The Id proteins perform their biological function via protein-protein interactions that involve not only class I and II bHLH proteins [ 61 – 63 ], but also proteins belonging to other families and containing other types of domains. These include the retinoblastoma protein tumor suppressor (pRb) and related pocket proteins [ 64 , 65 ], the actin-associated protein enigma homolog (ENH) [ 66 , 67 ], the p200 family member p204 [ 68 , 69 ], Ets-domain proteins [ 70 ], MIDA1 [ 71 , 72 ], Pax transcription factors [ 73 ], adenovirus E1A proteins [ 74 ], ADD1/SREBP-1c [ 75 ], the C8 subunit of the 20 S proteasome [ 76 ], the hepatitis B virus-encoded protein X (HBX) [ 76 ], the S5a subunit of the 26 S proteasome [ 77 ], the COP9 signalosome (CSN) subunits CSN5 and CSN7 [ 78 ], the deubiquitinase USP1 [ 79 ], the Apc/C subunits Apc1, Apc5, Apc8/Cdc23 [ 50 ], the cell-membrane protein caveolin-1 [ 80 ], the four-and-a-half LIM-only protein 2 (FHL2) [ 81 ], the Von-Hippel Lindau(VHL)-elongin-C complex [ 82 ], and the estrogen receptor beta-1 (ERβ1) [ 83 ] (Table 2 ). The fact that some of these interactions are specific for individual Id-family members suggests that they are not only mediated by the highly conserved HLH motif, but also by the less conserved N-terminal and C-terminal regions.…”

Section: Mode Of Actionmentioning

confidence: 99%

“…Indeed, it has been reported that in proliferating C2C12 myoblasts MyoD and Id1 are co-localized in the nucleus, while in differentiated myotubes MyoD is located in the nucleus and Id1 in the cytoplasm [ 186 ]. Furthermore, it has been observed, that Id2 reduces the myogenic markers MyoD and myogenin in myoblasts, however, ENH1 overexpression restores myogenic differentiation by binding Id2 [ 67 ].…”

Section: Myogenesismentioning

confidence: 99%

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The Id-protein family in developmental and cancer-associated pathways

2017

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Inhibitors of DNA binding and cell differentiation (Id) proteins are members of the large family of the helix-loop-helix (HLH) transcription factors, but they lack any DNA-binding motif. During development, the Id proteins play a key role in the regulation of cell-cycle progression and cell differentiation by modulating different cell-cycle regulators both by direct and indirect mechanisms. Several Id-protein interacting partners have been identified thus far, which belong to structurally and functionally unrelated families, including, among others, the class I and II bHLH transcription factors, the retinoblastoma protein and related pocket proteins, the paired-box transcription factors, and the S5a subunit of the 26 S proteasome. Although the HLH domain of the Id proteins is involved in most of their protein-protein interaction events, additional motifs located in their N-terminal and C-terminal regions are required for the recognition of diverse protein partners. The ability of the Id proteins to interact with structurally different proteins is likely to arise from their conformational flexibility: indeed, these proteins contain intrinsically disordered regions that, in the case of the HLH region, undergo folding upon self- or heteroassociation. Besides their crucial role for cell-fate determination and cell-cycle progression during development, other important cellular events have been related to the Id-protein expression in a number of pathologies. Dysregulated Id-protein expression has been associated with tumor growth, vascularization, invasiveness, metastasis, chemoresistance and stemness, as well as with various developmental defects and diseases. Herein we provide an overview on the structural properties, mode of action, biological function and therapeutic potential of these regulatory proteins.

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Section: Mode Of Actionmentioning

confidence: 99%

Section: Myogenesismentioning

confidence: 99%

The Id-protein family in developmental and cancer-associated pathways

2017

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“…The silencing of PDLIM5 increases the nuclear accumulation of differentiation inhibitor (Id2), which inhibits the proliferation and differentiation of myoblasts. Another protein, Fibrillin 1, was higher in KE mice and it influences the skeletal muscle stem cell microenvironment that interacts with bone ( 57 ). On the other hand, transgelin was lower in KE mice and previous studies have indicated overexpression or deficiency of transgelin results in significant changes in cell morphology, cytoskeleton, and functional capacity for migration that influence stem cell differentiation ( 58 ).…”

Section: Discussionmentioning

confidence: 99%

Effects of an exogenous ketone ester using multi-omics in skeletal muscle of aging C57BL/6J male mice

et al. 2022

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Exogenous ketone ester supplementation provides a means to increase circulating ketone concentrations without the dietary challenges imposed by ketogenic diets. Our group has shown that oral R,S-1,3, butanediol diacetoacetate (BD-AcAc2) consumption results in body weight loss or maintenance with moderate increases in circulating ketones. We have previously shown a diet consisting of 25% BD-AcAc2 can maintain lean body mass (LBM) and induce fat mass (FM) loss in young, healthy male mice, but the underlying mechanisms are still unknown. Therefore, the purpose of this study was to determine if a diet consisting of 25% BD-AcAc2 (ketone ester, KE) would alter body composition, transcriptional regulation, the proteome, and the lipidome of skeletal muscle in aged mice. We hypothesized that the KE group would remain weight stable with improvements in body composition compared to controls, resulting in a healthy aging phenotype. Male C57BL/6J mice (n = 16) were purchased from Jackson Laboratories at 72 weeks of age. After 1 week of acclimation, mice were weighed and randomly assigned to one of two groups (n = 8 per group): control (CON) or KE. A significant group by time interaction was observed for body weight (P < 0.001), with KE fed mice weighing significantly less than CON. FM increased over time in the control group but was unchanged in the KE group. Furthermore, LBM was not different between CON and KE mice despite KE mice weighing less than CON mice. Transcriptional analysis of skeletal muscle identified 6 genes that were significantly higher and 21 genes that were significantly lower in the KE group compared to CON. Lipidomic analysis of skeletal muscle identified no differences between groups for any lipid species, except for fatty acyl chains in triacylglycerol which was 46% lower in the KE group. Proteomics analysis identified 44 proteins that were different between groups, of which 11 were lower and 33 were higher in the KE group compared to CON. In conclusion, 72-week-old male mice consuming the exogenous KE, BD-AcAc2, had lower age-related gains in body weight and FM compared to CON mice. Furthermore, transcriptional and proteomics data suggest a signature in skeletal muscle of KE-treated mice consistent with markers of improved skeletal muscle regeneration, improved electron transport chain utilization, and increased insulin sensitivity.

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“…Myogenesis is an important biological process that underpins skeletal muscle regeneration and postnatal growth. The silencing of PDLIM5 increases the nuclear accumulation of differentiation inhibitor (Id2), which inhibits the proliferation and differentiation of myoblasts (Nakatani et al, 2016;Qiu et al, 2016). In addition, the differentiation of, and morphological changes in, skeletal muscle is regulated by a group of transcription factors known as myogenic regulators.…”

Section: Physiological Roles Of Pdlim5 In the Heartmentioning

confidence: 99%

An Overview of the Cytoskeleton-Associated Role of PDLIM5

Huang

Ouyang

et al. 2020

Front. Physiol.

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Regenerative medicine represented by stem cell technology has become one of the pillar medical technologies for human disease treatment. Cytoskeleton plays important roles in maintaining cell morphology, bearing external forces, and maintaining the effectiveness of cell internal structure, among which cytoskeleton related proteins are involved in and play an indispensable role in the changes of cytoskeleton. PDLIM5 is a cytoskeleton-related protein that, like other cytoskeletal proteins, acts as a binding protein. PDZ and LIM domain 5 (PDLIM5), also known as ENH (Enigma homolog), is a cytoplasmic protein with a molecular mass of about 63 KDa that consists of a PDZ domain at the N-terminus and three LIM domains at the C-terminus. PDLIM5 binds to the cytoskeleton and membrane proteins through its PDZ domain and interacts with various signaling molecules, including protein kinases and transcription factors, through its LIM domain. As a cytoskeleton-related protein, PDLIM5 plays an important role in regulating cell proliferation, differentiation and cell fate decision in multiple tissues and cell types. In this review, we briefly summarize the state of knowledge on the PDLIM5 gene, structural properties, and molecular functional mechanisms of the PDLIM5 protein, and its role in cells, tissues, and organ systems, and describe the possible underlying molecular signaling pathways. In the last part of this review, we will focus on discussing the limitations of existing research and the future prospects of PDLIM5 research in turn.

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Scaffold protein enigma homolog 1 overcomes the repression of myogenesis activation by inhibitor of DNA binding 2

Cited by 7 publications

References 35 publications

The Id-protein family in developmental and cancer-associated pathways

The Id-protein family in developmental and cancer-associated pathways

Effects of an exogenous ketone ester using multi-omics in skeletal muscle of aging C57BL/6J male mice

An Overview of the Cytoskeleton-Associated Role of PDLIM5

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