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Gene Review

CD2AP  -  CD2-associated protein

Homo sapiens

Synonyms: Adapter protein CMS, CMS, Cas ligand with multiple SH3 domains
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Disease relevance of CD2AP


Psychiatry related information on CD2AP

  • CMS rats spent more time in REM sleep and showed more fragmented sleep compared to their baseline recording, while there were no changes in the control rats [6].
  • In an animal model of depression, chronic exposure to mild stressors (CMS, e.g. periods of soiled cage, reversed light/dark cycle, grouped housing, food and/or water deprivation) causes behavioral and hormonal changes which, in humans, often are associated with depression [6].
  • Increased sleep fragmentation in CMS rats was particularly evident by increased number of arousals, and increased REM sleep and slow-wave-sleep-1 (SWS-1) episodes [6].
  • In fall 1998 CMS implemented the National Medicare Education Program (NMEP) to educate beneficiaries about their Medicare program benefits; health plan choices; supplemental health insurance; beneficiary rights, responsibilities, and protections; and health behaviors [7].

High impact information on CD2AP

  • This novel protein, called CD2AP, is likely to facilitate receptor patterning in the contact area by linking specific adhesion receptors to the cytoskeleton [8].
  • However, mRNA and protein levels for CD2AP and podocin were greatly reduced, suggesting a cooperative role for these molecules in foot process and slit diaphragm formation [9].
  • That podocin interacts with CD2AP and nephrin in vivo is shown by coimmunoprecipitation of these proteins from glomerular extracts [10].
  • Whether disruption in a particular mitochondrial function is at the root of CMS in all species, or whether defects in numerous mitochondrial activities can produce sterility, will only be revealed by further probing of physiological and biochemical defects present in CMS genotypes [11].
  • A characteristic of CMS mutations in plants, in contrast to the single base changes in human mitochondrial mutants (49, 140), is the presence of chimeric genes or chimeric loci; different open reading frames are joined together, or placed in proximal locations and cotranscribed with standard mitochondrial genes [11].

Chemical compound and disease context of CD2AP


Biological context of CD2AP


Anatomical context of CD2AP


Associations of CD2AP with chemical compounds


Physical interactions of CD2AP


Co-localisations of CD2AP

  • In conditionally immortalized mouse podocytes, we demonstrate that CD2AP colocalizes with cortactin and F-actin in spots of < or =0.5-microm diameter [26].

Regulatory relationships of CD2AP

  • CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl [19].

Other interactions of CD2AP

  • With the use of a conditionally immortalized human podocyte cell line, it first was shown that exposure to normal and non-nephrotic human plasma leads to a concentration of nephrin, podocin, CD2AP, and actin at the cell surface [18].
  • There are also 3 genetic loci connected with autosomal dominant forms of FSGS: ACTN4, TRPC6 and CD2AP (found only in the mice models) [27].
  • We propose that CD2AP/CMS, through interactions with Rab4 and c-Cbl, controls early endosome morphology and may play a role in traffic between early and late endosomes, and thus in the degradative pathway [19].
  • We have identified a novel c-Cbl-interacting protein termed CIN85 with a molecular mass of 85 kDa which shows similarity to adaptor proteins, CMS and CD2AP [28].
  • Secondary changes in the distribution of nephrin, CD2AP, and alpha-actinin are additional evidences for the scaffolding role of podocin in the organization of the slit diaphragm [29].

Analytical, diagnostic and therapeutic context of CD2AP


  1. Selective impairment of gene expression and assembly of nephrin in human diabetic nephropathy. Benigni, A., Gagliardini, E., Tomasoni, S., Abbate, M., Ruggenenti, P., Kalluri, R., Remuzzi, G. Kidney Int. (2004) [Pubmed]
  2. CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere. Li, C., Ruotsalainen, V., Tryggvason, K., Shaw, A.S., Miner, J.H. Am. J. Physiol. Renal Physiol. (2000) [Pubmed]
  3. CD2-associated protein and glomerular disease. Wolf, G., Stahl, R.A. Lancet (2003) [Pubmed]
  4. Role of podocyte slit diaphragm as a filtration barrier. Kawachi, H., Miyauchi, N., Suzuki, K., Han, G.D., Orikasa, M., Shimizu, F. Nephrology (Carlton, Vic.) (2006) [Pubmed]
  5. T-cell activation and immunologic synapse. Shaw, A.S. Immunol. Res. (2005) [Pubmed]
  6. Chronic mild stress affects sucrose intake and sleep in rats. Grønli, J., Murison, R., Bjorvatn, B., Sørensen, E., Portas, C.M., Ursin, R. Behav. Brain Res. (2004) [Pubmed]
  7. Lessons learned from the National Medicare & You Education Program. Goldstein, E., Teichman, L., Crawley, B., Gaumer, G., Joseph, C., Reardon, L. Health care financing review. (2001) [Pubmed]
  8. A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts. Dustin, M.L., Olszowy, M.W., Holdorf, A.D., Li, J., Bromley, S., Desai, N., Widder, P., Rosenberger, F., van der Merwe, P.A., Allen, P.M., Shaw, A.S. Cell (1998) [Pubmed]
  9. Transcriptional induction of slit diaphragm genes by Lmx1b is required in podocyte differentiation. Miner, J.H., Morello, R., Andrews, K.L., Li, C., Antignac, C., Shaw, A.S., Lee, B. J. Clin. Invest. (2002) [Pubmed]
  10. Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin. Schwarz, K., Simons, M., Reiser, J., Saleem, M.A., Faul, C., Kriz, W., Shaw, A.S., Holzman, L.B., Mundel, P. J. Clin. Invest. (2001) [Pubmed]
  11. Plant mitochondrial mutations and male sterility. Hanson, M.R. Annu. Rev. Genet. (1991) [Pubmed]
  12. WT1 mutations in nephrotic syndrome revisited. High prevalence in young girls, associations and renal phenotypes. Aucella, F., Bisceglia, L., De Bonis, P., Gigante, M., Caridi, G., Barbano, G., Mattioli, G., Perfumo, F., Gesualdo, L., Ghiggeri, G.M. Pediatr. Nephrol. (2006) [Pubmed]
  13. Nephrin and CD2AP associate with phosphoinositide 3-OH kinase and stimulate AKT-dependent signaling. Huber, T.B., Hartleben, B., Kim, J., Schmidts, M., Schermer, B., Keil, A., Egger, L., Lecha, R.L., Borner, C., Pavenstädt, H., Shaw, A.S., Walz, G., Benzing, T. Mol. Cell. Biol. (2003) [Pubmed]
  14. A Cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton. Lynch, D.K., Winata, S.C., Lyons, R.J., Hughes, W.E., Lehrbach, G.M., Wasinger, V., Corthals, G., Cordwell, S., Daly, R.J. J. Biol. Chem. (2003) [Pubmed]
  15. Clues to CD2-associated protein involvement in cytokinesis. Monzo, P., Gauthier, N.C., Keslair, F., Loubat, A., Field, C.M., Le Marchand-Brustel, Y., Cormont, M. Mol. Biol. Cell (2005) [Pubmed]
  16. Interaction of endogenous nephrin and CD2-associated protein in mouse epithelial M-1 cell line. Palmén, T., Lehtonen, S., Ora, A., Kerjaschki, D., Antignac, C., Lehtonen, E., Holthöfer, H. J. Am. Soc. Nephrol. (2002) [Pubmed]
  17. Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85. Hutchings, N.J., Clarkson, N., Chalkley, R., Barclay, A.N., Brown, M.H. J. Biol. Chem. (2003) [Pubmed]
  18. Nephrotic plasma alters slit diaphragm-dependent signaling and translocates nephrin, Podocin, and CD2 associated protein in cultured human podocytes. Coward, R.J., Foster, R.R., Patton, D., Ni, L., Lennon, R., Bates, D.O., Harper, S.J., Mathieson, P.W., Saleem, M.A. J. Am. Soc. Nephrol. (2005) [Pubmed]
  19. CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl. Cormont, M., Metón, I., Mari, M., Monzo, P., Keslair, F., Gaskin, C., McGraw, T.E., Le Marchand-Brustel, Y. Traffic (2003) [Pubmed]
  20. The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction. Kirsch, K.H., Georgescu, M.M., Shishido, T., Langdon, W.Y., Birge, R.B., Hanafusa, H. J. Biol. Chem. (2001) [Pubmed]
  21. The c-Cbl/CD2AP complex regulates VEGF-induced endocytosis and degradation of Flt-1 (VEGFR-1). Kobayashi, S., Sawano, A., Nojima, Y., Shibuya, M., Maru, Y. FASEB J. (2004) [Pubmed]
  22. Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin. Reiser, J., Oh, J., Shirato, I., Asanuma, K., Hug, A., Mundel, T.M., Honey, K., Ishidoh, K., Kominami, E., Kreidberg, J.A., Tomino, Y., Mundel, P. J. Biol. Chem. (2004) [Pubmed]
  23. Animal models of FSGS: lessons for pathogenesis and treatment. Fogo, A.B. Semin. Nephrol. (2003) [Pubmed]
  24. Priming of CD2-induced p62Dok tyrosine phosphorylation by CD3 in Jurkat T cells. Harriague, J., Debré, P., Bismuth, G., Hubert, P. Eur. J. Immunol. (2000) [Pubmed]
  25. Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Gaidos, G., Soni, S., Oswald, D.J., Toselli, P.A., Kirsch, K.H. J. Cell. Sci. (2007) [Pubmed]
  26. Association of CD2AP with dynamic actin on vesicles in podocytes. Welsch, T., Endlich, N., Gökce, G., Doroshenko, E., Simpson, J.C., Kriz, W., Shaw, A.S., Endlich, K. Am. J. Physiol. Renal Physiol. (2005) [Pubmed]
  27. Genetic basis of nephrotic syndrome--review. Obeidová, H., Merta, M., Reiterová, J., Maixnerová, D., Stekrová, J., Rysavá, R., Tesar, V. Prague medical report. (2006) [Pubmed]
  28. Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl. Take, H., Watanabe, S., Takeda, K., Yu, Z.X., Iwata, N., Kajigaya, S. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  29. In vivo expression of podocyte slit diaphragm-associated proteins in nephrotic patients with NPHS2 mutation. Zhang, S.Y., Marlier, A., Gribouval, O., Gilbert, T., Heidet, L., Antignac, C., Gubler, M.C. Kidney Int. (2004) [Pubmed]
  30. Early glomerular filtration defect and severe renal disease in podocin-deficient mice. Roselli, S., Heidet, L., Sich, M., Henger, A., Kretzler, M., Gubler, M.C., Antignac, C. Mol. Cell. Biol. (2004) [Pubmed]
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