2j6f Citations

Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain.

J. Biol. Chem. 281 38845-53 (2006)
Related entries: 2j6k, 2j7i, 2j6o

Cited: 23 times
EuropePMC logo PMID: 17020880


The CIN85/CMS (human homologs of mouse SH3KBP1/CD2AP) family of endocytic adaptor proteins has the ability to engage multiple effectors and couple cargo trafficking with the cytoskeleton. CIN85 and CMS (Cas ligand with multiple Src homology 3 (SH3) domains) facilitate the formation of large multiprotein complexes required for an efficient internalization of cell surface receptors. It has recently been shown that c-Cbl/Cbl-b could mediate the formation of a ternary complex between one c-Cbl/Cbl-b molecule and two SH3 domains of CIN85, important for the ability of Cbl to promote epidermal growth factor receptor down-regulation. To further investigate whether multimerization is conserved within the family of adaptor proteins, we have solved the crystal structures of the CMS N-terminal SH3 domain-forming complexes with Cbl-b- and CD2-derived peptides. Together with biochemical evidence, the structures support the notion that, despite clear differences in the interaction surface, both Cbl-b and CD2 can mediate multimerization of N-terminal CMS SH3 domains. Detailed analyses on the interacting surfaces also provide the basis for a differential Cbl-b molecular recognition of CMS and CIN85.

Reviews citing this publication (3)

  1. E3 ubiquitin ligase Cbl-b in innate and adaptive immunity. Liu Q, Zhou H, Langdon WY, Zhang J. Cell Cycle 13 1875-1884 (2014)
  2. SH3 domains: modules of protein-protein interactions. Kurochkina N, Guha U. Biophys Rev 5 29-39 (2013)
  3. Interfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein-protein interaction domains. Zafra-Ruano A, Luque I. FEBS Lett. 586 2619-2630 (2012)

Articles citing this publication (20)

  1. Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site. Usami Y, Popov S, Göttlinger HG. J. Virol. 81 6614-6622 (2007)
  2. Rosetta FlexPepDock ab-initio: simultaneous folding, docking and refinement of peptides onto their receptors. Raveh B, London N, Zimmerman L, Schueler-Furman O. PLoS ONE 6 e18934 (2011)
  3. Proteins recruited by SH3 domains of Ruk/CIN85 adaptor identified by LC-MS/MS. Havrylov S, Rzhepetskyy Y, Malinowska A, Drobot L, Redowicz MJ. Proteome Sci 7 21 (2009)
  4. CIN85 regulates dopamine receptor endocytosis and governs behaviour in mice. Shimokawa N, Haglund K, Hölter SM, Grabbe C, Kirkin V, Koibuchi N, Schultz C, Rozman J, Hoeller D, Qiu CH, Londoño MB, Ikezawa J, Jedlicka P, Stein B, Schwarzacher SW, Wolfer DP, Ehrhardt N, Heuchel R, Nezis I, Brech A, Schmidt MH, Fuchs H, Gailus-Durner V, Klingenspor M, Bogler O, Wurst W, Deller T, de Angelis MH, Dikic I. EMBO J. 29 2421-2432 (2010)
  5. Rac1 recruits the adapter protein CMS/CD2AP to cell-cell contacts. van Duijn TJ, Anthony EC, Hensbergen PJ, Deelder AM, Hordijk PL. J. Biol. Chem. 285 20137-20146 (2010)
  6. Bin1 SRC homology 3 domain acts as a scaffold for myofiber sarcomere assembly. Fernando P, Sandoz JS, Ding W, de Repentigny Y, Brunette S, Kelly JF, Kothary R, Megeney LA. J. Biol. Chem. 284 27674-27686 (2009)
  7. Functional diversity and structural disorder in the human ubiquitination pathway. Bhowmick P, Pancsa R, Guharoy M, Tompa P. PLoS ONE 8 e65443 (2013)
  8. The high resolution NMR structure of the third SH3 domain of CD2AP. Ortega Roldan JL, Romero Romero ML, Ora A, Ab E, Lopez Mayorga O, Azuaga AI, van Nuland NA. J. Biomol. NMR 39 331-336 (2007)
  9. Structure of Stenotrophomonas maltophilia FeoA complexed with zinc: a unique prokaryotic SH3-domain protein that possibly acts as a bacterial ferrous iron-transport activating factor. Su YC, Chin KH, Hung HC, Shen GH, Wang AH, Chou SH. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 636-642 (2010)
  10. High resolution crystal structures of the p120 RasGAP SH3 domain. Ross B, Kristensen O, Favre D, Walicki J, Kastrup JS, Widmann C, Gajhede M. Biochem. Biophys. Res. Commun. 353 463-468 (2007)
  11. The promiscuous binding of the Fyn SH3 domain to a peptide from the NS5A protein. Martin-Garcia JM, Luque I, Ruiz-Sanz J, Camara-Artigas A. Acta Crystallogr. D Biol. Crystallogr. 68 1030-1040 (2012)
  12. Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP. Roldan JL, Blackledge M, van Nuland NA, Azuaga AI. J. Biomol. NMR 50 103-117 (2011)
  13. Identification of CMS as a cytosolic adaptor of the human pTalpha chain involved in pre-TCR function. Navarro MN, Nusspaumer G, Fuentes P, González-García S, Alcain J, Toribio ML. Blood 110 4331-4340 (2007)
  14. Novel insights into the mechanisms of CIN85 SH3 domains binding to Cbl proteins: solution-based investigations and in vivo implications. Ababou A, Pfuhl M, Ladbury JE. J. Mol. Biol. 387 1120-1136 (2009)
  15. Inhibition of CIN85-mediated invasion by a novel SH3 domain binding motif in the lysyl oxidase propeptide. Sato S, Zhao Y, Imai M, Simister PC, Feller SM, Trackman PC, Kirsch KH, Sonenshein GE. PLoS ONE 8 e77288 (2013)
  16. A graph kernel approach for alignment-free domain-peptide interaction prediction with an application to human SH3 domains. Kundu K, Costa F, Backofen R. Bioinformatics 29 i335-43 (2013)
  17. The adapter protein CD2AP binds to p53 protein in the cytoplasm and can discriminate its polymorphic variants P72R. Panni S, Salvioli S, Santonico E, Langone F, Storino F, Altilia S, Franceschi C, Cesareni G, Castagnoli L. J. Biochem. 157 101-111 (2015)
  18. Multimeric and differential binding of CIN85/CD2AP with two atypical proline-rich sequences from CD2 and Cbl-b*. Ceregido MA, Garcia-Pino A, Ortega-Roldan JL, Casares S, López Mayorga O, Bravo J, van Nuland NA, Azuaga AI. FEBS J. 280 3399-3415 (2013)
  19. Structure of the kidney slit diaphragm adapter protein CD2-associated protein as determined with electron microscopy. Adair BD, Altintas MM, Möller CC, Arnaout MA, Reiser J. J. Am. Soc. Nephrol. 25 1465-1473 (2014)
  20. Differential Recognition Preferences of the Three Src Homology 3 (SH3) Domains from the Adaptor CD2-associated Protein (CD2AP) and Direct Association with Ras and Rab Interactor 3 (RIN3). Rouka E, Simister PC, Janning M, Kumbrink J, Konstantinou T, Muniz JR, Joshi D, O'Reilly N, Volkmer R, Ritter B, Knapp S, von Delft F, Kirsch KH, Feller SM. J. Biol. Chem. 290 25275-25292 (2015)