ArticleCell structure and function2023
Role of CRP2-MRTF interaction in functions of myofibroblasts.
Article in Cell structure and function, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Integrated single-cell and bulk RNA sequencing analysis establishes a cancer associated fibroblast-related signature for predicting prognosis and therapeutic responses in neuroblastoma.Discover oncology · 2025Article
- [Role and mechanism of cysteine and glycine-rich protein 2 in the malignant progression of neuroblastoma].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2024Article
- TGF-β signaling promotes desmoid tumor formation via CSRP2 upregulation.Cancer science · 2024Article
- Significance of the p38MAPK-CRP2 axis in myofibroblastic phenotypic transition.Cell structure and function · 2023Article
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Authors and funding
12 authors at 5 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Inflammatory response induces phenotypic modulation of fibroblasts into myofibroblasts. Although transforming growth factor-βs (TGF-βs) evoke such transition, the details of the mechanism are still unknown. Here, we report that a LIM domain protein, cysteine-and glycine-rich protein 2 (CSRP2 [CRP2]) plays a vital role in the functional expression profile in myofibroblasts and cancer-associated fibroblasts (CAFs). Knock-down of CRP2 severely inhibits the expression of smooth muscle cell (SMC) genes, cell motility, and CAF-mediated collective invasion of epidermoid carcinoma. We elucidate the following molecular bases: CRP2 directly binds to myocardin-related transcription factors (MRTF-A/B [MRTFs]) and serum response factor (SRF) and stabilizes the MRTF/SRF/CArG-box complex to activate SMC gene expression. Furthermore, a three-dimensional structural analysis of CRP2 identifies the amino acids required for the CRP2-MRTF-A interaction. Polar amino acids in the C-terminal half (serine-152, glutamate-154, serine-155, threonine-156, threonine-157, and threonine-159 in human CRP2) are responsible for direct binding to MRTF-A. On the other hand, hydrophobic amino acids outside the consensus sequence of the LIM domain (tryptophan-139, phenylalanine-144, leucine-153, and leucine-158 in human CRP2) play a role in stabilizing the unique structure of the LIM domain.Key words: CRP2, 3D structure, myocardin-related transcription factor, myofibroblast, cancer-associated fibroblasts.
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