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Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3.

Bouyain S, Leahy DJ
Protein Sci 16 654-61 (2007)
Cited: 16 times
EuropePMC logo PMID: 17384230

Abstract

The E3 ubiquitin ligase neuregulin receptor degrading protein 1 (Nrdp1) mediates the ligand-independent degradation of the epidermal growth factor receptor family member ErbB3/HER3. By regulating cellular levels of ErbB3, Nrdp1 influences ErbB3-mediated signaling, which is essential for normal vertebrate development. Nrdp1 belongs to the tripartite or RBCC (RING, B-box, coiled-coil) family of ubiquitin ligases in which the RING domain is responsible for ubiquitin ligation and a variable C-terminal region mediates substrate recognition. We report here the 1.95 A crystal structure of the C-terminal domain of Nrdp1 and show that this domain is sufficient to mediate ErbB3 binding. Furthermore, we have used site-directed mutagenesis to map regions of the Nrdp1 surface that are important for interacting with ErbB3 and mediating its degradation in transfected cells. The ErbB3-binding site localizes to a region of Nrdp1 that is conserved from invertebrates to vertebrates, in contrast to ErbB3, which is only found in vertebrates. This observation suggests that Nrdp1 uses a common binding site to recognize its targets in different species.

Articles - 2ogb mentioned but not cited (1)

  1. Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3. Bouyain S, Leahy DJ. Protein Sci 16 654-661 (2007)


Reviews citing this publication (3)

  1. Targeting ubiquitination for cancer therapies. Morrow JK, Lin HK, Sun SC, Zhang S. Future Med Chem 7 2333-2350 (2015)
  2. The role of ErbB3 and its binding partners in breast cancer progression and resistance to hormone and tyrosine kinase directed therapies. Hamburger AW. J Mammary Gland Biol Neoplasia 13 225-233 (2008)
  3. E3 ubiquitin ligases in ErbB receptor quantity control. Carraway KL. Semin Cell Dev Biol 21 936-943 (2010)

Articles citing this publication (12)

  1. Pharmacological targeting of the pseudokinase Her3. Xie T, Lim SM, Westover KD, Dodge ME, Ercan D, Ficarro SB, Udayakumar D, Gurbani D, Tae HS, Riddle SM, Sim T, Marto JA, Jänne PA, Crews CM, Gray NS. Nat Chem Biol 10 1006-1012 (2014)
  2. The E3 ubiquitin ligase NEDD4 negatively regulates HER3/ErbB3 level and signaling. Huang Z, Choi BK, Mujoo K, Fan X, Fa M, Mukherjee S, Owiti N, Zhang N, An Z. Oncogene 34 1105-1115 (2015)
  3. An E3 ubiquitin ligase, Really Interesting New Gene (RING) Finger 41, is a candidate gene for anxiety-like behavior and beta-carboline-induced seizures. Kim S, Zhang S, Choi KH, Reister R, Do C, Baykiz AF, Gershenfeld HK. Biol Psychiatry 65 425-431 (2009)
  4. Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues. Nikolaienko RM, Hammel M, Dubreuil V, Zalmai R, Hall DR, Mehzabeen N, Karuppan SJ, Harroch S, Stella SL, Bouyain S. J Biol Chem 291 21335-21349 (2016)
  5. The anti-HER3 (ErbB3) therapeutic antibody 9F7-F11 induces HER3 ubiquitination and degradation in tumors through JNK1/2- dependent ITCH/AIP4 activation. Le Clorennec C, Lazrek Y, Dubreuil O, Larbouret C, Poul MA, Mondon P, Melino G, Pèlegrin A, Chardès T. Oncotarget 7 37013-37029 (2016)
  6. Phosphorylation of the E3 ubiquitin ligase RNF41 by the kinase Par-1b is required for epithelial cell polarity. Lewandowski KT, Piwnica-Worms H. J Cell Sci 127 315-327 (2014)
  7. Oligomerization of the Nrdp1 E3 ubiquitin ligase is necessary for efficient autoubiquitination but not ErbB3 ubiquitination. Printsev I, Yen L, Sweeney C, Carraway KL. J Biol Chem 289 8570-8578 (2014)
  8. The ER structural protein Rtn4A stabilizes and enhances signaling through the receptor tyrosine kinase ErbB3. Hatakeyama J, Wald JH, Rafidi H, Cuevas A, Sweeney C, Carraway KL. Sci Signal 9 ra65 (2016)
  9. ERBB3: A potential serum biomarker for early detection and therapeutic target for devil facial tumour 1 (DFT1). Hayes DA, Kunde DA, Taylor RL, Pyecroft SB, Sohal SS, Snow ET. PLoS One 12 e0177919 (2017)
  10. RNF41 interacts with the VPS52 subunit of the GARP and EARP complexes. Masschaele D, De Ceuninck L, Wauman J, Defever D, Stenner F, Lievens S, Peelman F, Tavernier J. PLoS One 12 e0178132 (2017)
  11. RNF41 regulates the damage recognition receptor Clec9A and antigen cross-presentation in mouse dendritic cells. Tullett KM, Tan PS, Park HY, Schittenhelm RB, Michael N, Li R, Policheni AN, Gruber E, Huang C, Fulcher AJ, Danne JC, Czabotar PE, Wakim LM, Mintern JD, Ramm G, Radford KJ, Caminschi I, O'Keeffe M, Villadangos JA, Wright MD, Blewitt ME, Heath WR, Shortman K, Purcell AW, Nicola NA, Zhang JG, Lahoud MH. Elife 9 e63452 (2020)
  12. Nrdp1-mediated degradation of BRUCE decreases cell viability and induces apoptosis in human 786-O renal cell carcinoma cells. Chen SJ, Lin JH, Yao XD, Peng B, Xu YF, Liu M, Zheng JH. Exp Ther Med 12 597-602 (2016)


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