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XIN-HUA FENG

TitleProfessor
InstitutionBaylor College of Medicine
DepartmentDepartment of Molecular & Cellular Biology
AddressOne Baylor Plaza, BCM-Alkek for Biomedical Research To
Houston TX 77030
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    Other Positions
    TitleProfessor
    InstitutionBaylor College of Medicine
    DepartmentDepartment of Surgery
    DivisionSurgery-Surgical Research

    TitleProfessor
    InstitutionBaylor College of Medicine


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    Collapse Biography 
    Collapse awards and honors
    2001Keck Young Scholar Research Achievement Award, W.M. Keck Foundation
    2003 - 2007American Cancer Society Research Scholar, American Cancer Society
    2003 - 2008The Leukemia & Lymphoma Society Scholar, The Leukemia & Lymphoma Society
    2006The Michael E. DeBakey Research in Excellence Award, Baylor College of Medicine
    2007Research in Excellence Award, BCM-Molecular & Cellular Biology
    2012AAAS Fellow, American Association for the Advancement of Science

    Collapse Overview 
    Collapse overview
    Dr. Feng’s research aims to elucidate the underlying mechanisms and interplays among protein modifications, signaling pathways, and gene transcription as well as understanding their roles in cell proliferation, tissue differentiation, and pathogenesis of human diseases.

    His current research projects include:
    Phosphatome: genome-wide investigation of protein dephosphorylation
    Signal transduction pathways are often regulated by the dynamic interplay between protein
    kinases and phosphatases. Using all the human protein serine/threonine phosphatases available, we systematically investigate the effect of dephosphorylation on key proteins involved in cell signaling and cell functions. We are currently genetically disrupting individual phosphatases to elucidate their in vivo functions during development.

    SUMO, ubiquitin, and control of protein turnover and functions

    We examine the effect of post-translational modifications, particularly ubiquitination and
    SUMOylation of transcription factors, in normal and cancer cells. We attempt to understand the molecular mechanisms by which environmental and developmental cues regulate the ubiquitination/proteasome and SUMOylation systems. Our studies will provide insights into the relationships between protein deregulation and human cancers or abnormal development.

    TGF-ß/BMP signal transduction

    SMADs are evolutionarily conserved signal transducers and transcription factors controlling
    TGF-ß/BMP functions. A large number of mutations that inactivate SMADs have been linked to human cancers and genetic diseases. We address the molecular interactions, requirements, and functionality of SMADs in TGF-ß/BMP responses using cellular, genomic, and proteomic approaches. We investigate how SMADs mediate transcription and how their actions are terminated. We also use in vitro and in vivo model systems to study how SMADs as tumor suppressors interplay with oncogenic pathways, in particular with those involved in lymphoma and in pancreatic and breast cancer.

    Genetic screens, BMP/TGF-ß signaling, and ES cells

    We are conducting genome-wide studies (e.g. genetic screens using lentiviral RNAi library) to
    identify novel TGF-ß signal modifiers or regulators involved in stem cell differentiation. Novel molecules that control TGF-ß/BMP signaling or participate in human ES cell self-renewal and differentiation will be further studied and in model organisms to define the molecules’ physiological roles in tissue differentiation and organ development.

    Immune suppression by TGF-ß

    TGF-ß is a major inflammatory and immune-regulatory cytokine, but the mechanisms by which
    TGF-ß exerts its actions are unclear. We are interested in investigating the signaling interactions between the TGF-ß pathway and other cytokine pathways (such as TNF-alpha, IL-1, and IL-6 pathways) in immune responses. This area of research may lead to the discovery of drugs to treat cancer and inflammatory diseases.

    Collapse keywords
    Embryonic stem cells, Serine/threonine phosphatases, SMAD, SUMOylation TGF-beta, Ubiquitination


    Collapse Bibliographic 
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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
    List All   |   Timeline
    1. Chen W, Wu J, Li L, Zhang Z, Ren J, Liang Y, Chen F, Yang C, Zhou Z, Su SS, Zheng X, Zhang Z, Zhong CQ, Wan H, Xiao M, Lin X, Feng XH, Han J. Ppm1b negatively regulates necroptosis through dephosphorylating Rip3. Nat Cell Biol. 2015 Apr; 17(4):434-44. PMID: 25751141.
      View in: PubMed
    2. Chen F, Lin X, Xu P, Zhang Z, Chen Y, Wang C, Han J, Zhao B, Xiao M, Feng XH. Nuclear Export of Smads by RanBP3L Regulates Bone Morphogenetic Protein Signaling and Mesenchymal Stem Cell Differentiation. Mol Cell Biol. 2015 May; 35(10):1700-11. PMID: 25755279.
      View in: PubMed
    3. Zhao Y, Xiao M, Sun B, Zhang Z, Shen T, Duan X, Yu PB, Feng XH, Lin X. C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via Smad dephosphorylation. J Biol Chem. 2014 Sep 19; 289(38):26441-50. PMID: 25100727; PMCID: PMC4176200.
    4. Shen T, Sun C, Zhang Z, Xu N, Duan X, Feng XH, Lin X. Specific control of BMP signaling and mesenchymal differentiation by cytoplasmic phosphatase PPM1H. Cell Res. 2014 Jun; 24(6):727-41. PMID: 24732009; PMCID: PMC4042171.
    5. Chen J, Xia Y, Lin X, Feng XH, Wang Y. Smad3 signaling activates bone marrow-derived fibroblasts in renal fibrosis. Lab Invest. 2014 May; 94(5):545-56. PMID: 24614197; PMCID: PMC4006302.
    6. Feng Y, Wu H, Xu Y, Zhang Z, Liu T, Lin X, Feng XH. Zinc finger protein 451 is a novel Smad corepressor in transforming growth factor-? signaling. J Biol Chem. 2014 Jan 24; 289(4):2072-83. PMID: 24324267; PMCID: PMC3900955.
    7. Wang A, Pan D, Lee YH, Martinez GJ, Feng XH, Dong C. Cutting edge: Smad2 and Smad4 regulate TGF-?-mediated Il9 gene expression via EZH2 displacement. J Immunol. 2013 Nov 15; 191(10):4908-12. PMID: 24108699; PMCID: PMC3842015.
    8. Zhou G, Wang H, Liu SH, Shahi KM, Lin X, Wu J, Feng XH, Qin J, Tan TH, Brunicardi FC. p38 MAP kinase interacts with and stabilizes pancreatic and duodenal homeobox-1. Curr Mol Med. 2013 Mar; 13(3):377-86. PMID: 23331010.
      View in: PubMed
    9. Qin J, Wu SP, Creighton CJ, Dai F, Xie X, Cheng CM, Frolov A, Ayala G, Lin X, Feng XH, Ittmann MM, Tsai SJ, Tsai MJ, Tsai SY. COUP-TFII inhibits TGF-?-induced growth barrier to promote prostate tumorigenesis. Nature. 2013 Jan 10; 493(7431):236-40. PMID: 23201680; PMCID: PMC4022346.
    10. Jia S, Dai F, Wu D, Lin X, Xing C, Xue Y, Wang Y, Xiao M, Wu W, Feng XH, Meng A. Protein phosphatase 4 cooperates with Smads to promote BMP signaling in dorsoventral patterning of zebrafish embryos. Dev Cell. 2012 May 15; 22(5):1065-78. PMID: 22595677.
      View in: PubMed
    11. Dai F, Shen T, Li Z, Lin X, Feng XH. PPM1A dephosphorylates RanBP3 to enable efficient nuclear export of Smad2 and Smad3. EMBO Rep. 2011 Nov; 12(11):1175-81. PMID: 21960005; PMCID: PMC3207100.
    12. Liu T, Feng XH. Regulation of TGF-beta signalling by protein phosphatases. Biochem J. 2010 Sep 1; 430(2):191-8. PMID: 20704570; PMCID: PMC3154754.
    13. Dai F, Duan X, Liang YY, Lin X, Feng XH. Coupling of dephosphorylation and nuclear export of Smads in TGF-beta signaling. Methods Mol Biol. 2010; 647:125-37. PMID: 20694664; PMCID: PMC3153448.
    14. Dai F, Lin X, Chang C, Feng XH. Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling. Dev Cell. 2009 Mar; 16(3):345-57. PMID: 19289081; PMCID: PMC2676691.
    15. Wrighton KH, Lin X, Feng XH. Phospho-control of TGF-beta superfamily signaling. Cell Res. 2009 Jan; 19(1):8-20. PMID: 19114991; PMCID: PMC2929013.
    16. Wrighton KH, Dai F, Feng XH. A new kid on the TGFbeta block: TAZ controls Smad nucleocytoplasmic shuttling. Dev Cell. 2008 Jul; 15(1):8-10. PMID: 18606136.
      View in: PubMed
    17. Wrighton KH, Feng XH. To (TGF)beta or not to (TGF)beta: fine-tuning of Smad signaling via post-translational modifications. Cell Signal. 2008 Sep; 20(9):1579-91. PMID: 18387785; PMCID: PMC2597537.
    18. Wang D, Long J, Dai F, Liang M, Feng XH, Lin X. BCL6 represses Smad signaling in transforming growth factor-beta resistance. Cancer Res. 2008 Feb 1; 68(3):783-9. PMID: 18245479.
      View in: PubMed
    19. Dai F, Chang C, Lin X, Dai P, Mei L, Feng XH. Erbin inhibits transforming growth factor beta signaling through a novel Smad-interacting domain. Mol Cell Biol. 2007 Sep; 27(17):6183-94. PMID: 17591701; PMCID: PMC1952163.
    20. Zhang S, Fei T, Zhang L, Zhang R, Chen F, Ning Y, Han Y, Feng XH, Meng A, Chen YG. Smad7 antagonizes transforming growth factor beta signaling in the nucleus by interfering with functional Smad-DNA complex formation. Mol Cell Biol. 2007 Jun; 27(12):4488-99. PMID: 17438144; PMCID: PMC1900056.
    21. Duan X, Liang YY, Feng XH, Lin X. Protein serine/threonine phosphatase PPM1A dephosphorylates Smad1 in the bone morphogenetic protein signaling pathway. J Biol Chem. 2006 Dec 1; 281(48):36526-32. PMID: 16931515.
      View in: PubMed
    22. Lin X, Duan X, Liang YY, Su Y, Wrighton KH, Long J, Hu M, Davis CM, Wang J, Brunicardi FC, Shi Y, Chen YG, Meng A, Feng XH. PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. Cell. 2006 Jun 2; 125(5):915-28. PMID: 16751101.
      View in: PubMed
    23. Lin X, Feng XH. Design and application of a versatile expression vector for RNAi in mammalian cells. J RNAi Gene Silencing. 2005; 1(1):38-43. PMID: 19771203; PMCID: PMC2737199.
    24. Feng XH, Derynck R. Specificity and versatility in tgf-beta signaling through Smads. Annu Rev Cell Dev Biol. 2005; 21:659-93. PMID: 16212511.
      View in: PubMed
    25. Miura M, Chen XD, Allen MR, Bi Y, Gronthos S, Seo BM, Lakhani S, Flavell RA, Feng XH, Robey PG, Young M, Shi S. A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells. J Clin Invest. 2004 Dec; 114(12):1704-13. PMID: 15599395; PMCID: PMC535063.
    26. Brown CO, Chi X, Garcia-Gras E, Shirai M, Feng XH, Schwartz RJ. The cardiac determination factor, Nkx2-5, is activated by mutual cofactors GATA-4 and Smad1/4 via a novel upstream enhancer. J Biol Chem. 2004 Mar 12; 279(11):10659-69. PMID: 14662776.
      View in: PubMed
    27. Lin X, Liang YY, Sun B, Liang M, Shi Y, Brunicardi FC, Shi Y, Feng XH. Smad6 recruits transcription corepressor CtBP to repress bone morphogenetic protein-induced transcription. Mol Cell Biol. 2003 Dec; 23(24):9081-93. PMID: 14645520; PMCID: PMC309600.
    28. Lin X, Liang M, Liang YY, Brunicardi FC, Melchior F, Feng XH. Activation of transforming growth factor-beta signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4. J Biol Chem. 2003 May 23; 278(21):18714-9. PMID: 12621041.
      View in: PubMed
    29. Berger DH, Feng XH, Yao J, Saha D, Beauchamp RD, Lin X. Resistance to transforming growth factor-beta occurs in the presence of normal Smad activation. Surgery. 2002 Aug; 132(2):310-6. PMID: 12219028.
      View in: PubMed
    30. Feng XH, Liang YY, Liang M, Zhai W, Lin X. Direct interaction of c-Myc with Smad2 and Smad3 to inhibit TGF-beta-mediated induction of the CDK inhibitor p15(Ink4B). Mol Cell. 2002 Jan; 9(1):133-43. PMID: 11804592.
      View in: PubMed
    31. Lin X, Liang M, Feng XH. Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling. J Biol Chem. 2000 Nov 24; 275(47):36818-22. PMID: 11016919.
      View in: PubMed
    32. Dong C, Li Z, Alvarez R, Feng XH, Goldschmidt-Clermont PJ. Microtubule binding to Smads may regulate TGF beta activity. Mol Cell. 2000 Jan; 5(1):27-34. PMID: 10678166.
      View in: PubMed
    33. Derynck R, Feng XH. TGF-beta receptor signaling. Biochim Biophys Acta. 1997 Oct 24; 1333(2):F105-50. PMID: 9395284.
      View in: PubMed
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