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DAPP1  -  dual adaptor of phosphotyrosine and 3...

Homo sapiens

Synonyms: B lymphocyte adapter protein Bam32, B-cell adapter molecule of 32 kDa, BAM32, Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide, HSPC066, ...
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Psychiatry related information on DAPP1

  • Initially the birds displayed motor activity only during the 8-hour DAPP [1].
  • Dependent personality disorder patients scored significantly higher on DAPP-BQ Insecure Attachment, and lower on DAPP Stimulus Seeking, Callousness, Intimacy Problems, and Conduct Problems compared to the healthy controls and all other patient groups [2].

High impact information on DAPP1

  • Daily 20-hour encephalic photophases (DEPP), transmitted (hours 0 to 20) via chronically implanted light-conducting fibers to selected sites in the basal hypothalamus of male white-crowned sparrows, were superimposed on daily 8-hour (hours 0 to 8) external ambient photophases (DAPP) [1].
  • To further define the role Bam32 plays in B cells, we generated Bam32-deficient DT40 cells [3].
  • These Bam32(-/-) cells exhibited lower levels of B cell antigen receptor (BCR)-induced calcium mobilization with modest decreases in tyrosine phosphorylation of phospholipase C (PLC)gamma 2 [3].
  • The B lymphocyte-associated adaptor protein 32 kD in size (Bam32) is expressed at high levels in germinal center (GC) B cells [3].
  • Activation of downstream transcription factors such as nuclear factor of activated T cells (NF-AT) and nuclear factor of kappa binding (NF-kappa B) was also impaired in Bam32(-/-) cells [3].

Biological context of DAPP1

  • Src, Lyn and Lck tyrosine kinases phosphorylate DAPP1 at Tyr(139) in vitro at similar rates in the presence or absence of PtdIns(3,4,5)P(3), and overexpression of these kinases in HEK-293 cells induces the phosphorylation of Tyr(139) [4].
  • We recently identified a novel adaptor protein, termed dual adaptor for phosphotyrosine and 3-phosphoinositides (DAPP1), that possesses a Src homology (SH2) domain and a pleckstrin homology (PH) domain [4].
  • Taken together, these findings suggest that Bam32 functions to regulate BCR-induced signaling and cell survival most likely in germinal centers [3].
  • We have identified and characterized a novel src homology 2 (SH2) and pleckstrin homology (PH) domain-containing adaptor protein, designated Bam32 (for B cell adaptor molecule of 32 kD). cDNAs encoding the human and mouse Bam32 coding sequences were isolated and the human bam32 gene was mapped to chromosome 4q25-q27 [5].
  • We report the characterization of two signal transduction proteins related to Bam32, known as TAPP1 and TAPP2 [6].

Anatomical context of DAPP1

  • These findings indicate that, following activation of PI 3-kinases, PtdIns(3,4,5)P(3) or PtdIns(3,4)P(2) bind to DAPP1, recruiting it to the plasma membrane where it becomes phosphorylated at Tyr(139) by a Src-family tyrosine kinase [4].
  • Regulation of B-lymphocyte activation by the PH domain adaptor protein Bam32/DAPP1 [7].
  • These results suggest that Bam32 regulates the cytoskeleton through Rac1 [8].
  • The positive and negative effects of Bam32 variants on F-actin levels were closely mirrored by their effects on the activation of the GTPase Rac1, which is known to regulate actin remodeling in lymphocytes [8].
  • BCR ligation induced colocalization of Bam32 with lipid rafts, clathrin, and actin filaments [9].

Associations of DAPP1 with chemical compounds

  • These observations predict that DAPP1 will interact with both tyrosine phosphorylated proteins and 3-phosphoinositides and may therefore play a role in regulating the location and/or activity of such proteins(s) in response to agonists that elevate PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2) [10].
  • DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides [10].
  • The structure is similar to the known structure of the PH domain of DAPP1 around the D-3 and D-4 inositol-phosphate-binding sites [11].
  • Many of these proteins, such as protein kinase B, phosphoinositide-dependent kinase 1 and the dual adaptor for phosphotyrosine and 3-phosphoinositides (DAPP1) interact with both PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2) with similar affinity [11].
  • However, a glycine residue adjacent to the D-5 inositol-phosphate-binding site in DAPP1 is substituted for a larger alanine residue in TAPP1, which also induces a conformational change in the neighbouring residues [11].

Physical interactions of DAPP1

  • Collectively, these findings indicate a novel role of Bam32 in connecting Src family PTKs to BCR internalization by an actin-dependent mechanism [9].

Other interactions of DAPP1

  • These data suggest that Bam32 functions downstream of Src family PTKs to regulate BCR internalization [9].
  • Bam32 contains one Src homology 2 and one pleckstrin homology domain and is phosphorylated at a single site, tyrosine 139 [8].
  • The B lymphocyte adaptor molecule of 32 kDa (Bam32) is an adaptor that plays an indispensable role in BCR signaling [9].
  • Strikingly, peroxide co-stimulation enhanced antigen receptor-induced membrane recruitment of Bam32 and TAPP2, with combined stimulation exceeding the maximum achievable with either stimulus alone [12].

Analytical, diagnostic and therapeutic context of DAPP1

  • Bam32 is tyrosine-phosphorylated upon B cell antigen receptor (BCR) ligation or pervanadate stimulation and associates with phospholipase Cgamma2 [5].
  • Two novel radioligands, N,N-dimethyl-2-(2-amino-4-methoxyphenylthio) b enzylamine (DAPP) and (N,N-dimethyl-2-(2-amino-4-cyanophenylthio) benzylamine (D ASB), were radiolabeled with carbon-11 and evaluated as in vivo probes of the serotonin transporter (SERT) using positron emission tomography (PET) [13].


  1. Induction of Zugunruhe by photostimulation of encephalic receptors in white-crowned sparrows. Yokoyama, K., Farner, D.S. Science (1978) [Pubmed]
  2. Line bisection performance in patients with personality disorders. Wang, W., Wang, Y., Gu, J., Drake, R.A., Livesley, W.J., Jang, K.L. Cognitive neuropsychiatry. (2003) [Pubmed]
  3. The B lymphocyte adaptor molecule of 32 kD (Bam32) regulates B cell antigen receptor signaling and cell survival. Niiro, H., Maeda, A., Kurosaki, T., Clark, E.A. J. Exp. Med. (2002) [Pubmed]
  4. Phosphoinositide 3-kinase-dependent phosphorylation of the dual adaptor for phosphotyrosine and 3-phosphoinositides by the Src family of tyrosine kinase. Dowler, S., Montalvo, L., Cantrell, D., Morrice, N., Alessi, D.R. Biochem. J. (2000) [Pubmed]
  5. A novel B lymphocyte-associated adaptor protein, Bam32, regulates antigen receptor signaling downstream of phosphatidylinositol 3-kinase. Marshall, A.J., Niiro, H., Lerner, C.G., Yun, T.J., Thomas, S., Disteche, C.M., Clark, E.A. J. Exp. Med. (2000) [Pubmed]
  6. TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma membrane recruitment triggered by the B-cell antigen receptor. Marshall, A.J., Krahn, A.K., Ma, K., Duronio, V., Hou, S. Mol. Cell. Biol. (2002) [Pubmed]
  7. Regulation of B-lymphocyte activation by the PH domain adaptor protein Bam32/DAPP1. Marshall, A.J., Zhang, T., Al-Alwan, M. Biochem. Soc. Trans. (2007) [Pubmed]
  8. The adaptor protein Bam32 regulates Rac1 activation and actin remodeling through a phosphorylation-dependent mechanism. Allam, A., Niiro, H., Clark, E.A., Marshall, A.J. J. Biol. Chem. (2004) [Pubmed]
  9. The B lymphocyte adaptor molecule of 32 kilodaltons (Bam32) regulates B cell antigen receptor internalization. Niiro, H., Allam, A., Stoddart, A., Brodsky, F.M., Marshall, A.J., Clark, E.A. J. Immunol. (2004) [Pubmed]
  10. DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides. Dowler, S., Currie, R.A., Downes, C.P., Alessi, D.R. Biochem. J. (1999) [Pubmed]
  11. Crystal structure of the phosphatidylinositol 3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): molecular basis of lipid specificity. Thomas, C.C., Dowler, S., Deak, M., Alessi, D.R., van Aalten, D.M. Biochem. J. (2001) [Pubmed]
  12. Regulation of phosphoinositide 3-kinase signaling by oxidants: Hydrogen peroxide selectively enhances immunoreceptor-induced recruitment of phosphatidylinositol (3,4) bisphosphate-binding PH domain proteins. Cheung, S.M., Kornelson, J.C., Al-Alwan, M., Marshall, A.J. Cell. Signal. (2007) [Pubmed]
  13. Imaging the serotonin transporter with positron emission tomography: initial human studies with [11C]DAPP and [11C]DASB. Houle, S., Ginovart, N., Hussey, D., Meyer, J.H., Wilson, A.A. European journal of nuclear medicine. (2000) [Pubmed]
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