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Gene Review

PDZK1IP1  -  PDZK1 interacting protein 1

Homo sapiens

Synonyms: 17 kDa membrane-associated protein, DD96, MAP17, PDZK1-interacting protein 1, Protein DD96, ...
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Disease relevance of PDZK1IP1

  • The protein cluster formed by PDZK1, MAP17, and cMOAT is upregulated in a significant number of human carcinomas originating in the colon, breast, lung, and kidney [1].
  • Immunhistologic staining of frozen sections derived from lesional skin of bullous pemphigoid und pemphigus vulgaris indicated that pKe#192/MAP17 was upregulated in the epidermis adjacent to the blister [2].
  • Taken together, our data show an independent activation of MAP17 promoter that can be driven by oncogenes and that might explain the common overexpression of MAP17 in human carcinomas [3].

High impact information on PDZK1IP1

  • Our results show striking coexpression of SCL and its immediate downstream neighbor, MAP17, suggesting that they share regulatory elements [4].
  • Our data show conserved synteny between zebrafish and mammalian SCL and MAP17 loci, thus suggesting the likely genomic domain necessary for the conserved pattern of SCL expression [5].
  • However, MAP17 is expressed abundantly in carcinomas arising from kidney, colon, lung, and breast, in some cases with a membrane-associated apical glandular distribution [6].
  • In normal tissues, MAP17 is expressed in significant amounts only in the kidney, where it was localized to the brush border of proximal tubular epithelial cells [6].
  • In tissue culture, MAP17 was localized to the cell membrane in areas of cell-cell contact, ie, the distribution of cell-function-associated proteins [6].

Biological context of PDZK1IP1

  • Finally, cotransfection of MAP17 and NHERF3 prevented the adaptive upregulation of phosphate transport activity in OK cells in response to low extracellular phosphate [7].
  • Transfection of MAP17 into the HT29 carcinoma cell line markedly decreased cell proliferation in vitro and tumor growth in vivo, suggesting that MAP17 plays a role, either direct or indirect, in the control of cell proliferation [8].
  • In an attempt to elucidate the function of MAP17, we screened a human kidney cDNA library for interacting proteins using the yeast two-hybrid system and isolated a novel protein containing PDZ protein interaction domains, which we have named PDZK1 [8].
  • PDZK1 may represent the link between the cell membrane-where it interacts with MAP17-and other cytoplasmic proteins involved in biologic functions such as cell proliferation, differentiation, and ion transport [8].

Anatomical context of PDZK1IP1

  • The membrane-associated protein pKe#192/MAP17 in human keratinocytes [2].
  • Rat kidney MAP17 induces cotransport of Na-mannose and Na-glucose in Xenopus laevis oocytes [9].
  • MAP17 is responsible for mannose transport expression in oocytes by rat kidney cortex mRNA [9].
  • Anti-SPAP antibodies visualized by secondary fluorescein isothiocyanate (FITC)-labelled antibodies were bound to the postacrosomal part of the spermatozoa, indicating that SPAP is specifically bound to this area, and directly interacts with the spermatozoa [10].

Associations of PDZK1IP1 with chemical compounds


Physical interactions of PDZK1IP1

  • Results obtained by various in vitro analyses suggested that MAP17 interacts with the fourth domain of PDZK1 but not with other PDZ proteins localized in proximal tubular brush borders [11].

Other interactions of PDZK1IP1

  • Unexpectedly, we found that hepatic overexpression of SPAP in mice resulted in liver deficiency of PDZK1 [12].
  • The interactions of MAP17 with the NHERF proteins and with NaPiIIa were further analyzed in opossum kidney (OK) cells [7].

Analytical, diagnostic and therapeutic context of PDZK1IP1


  1. Targeted disruption of the PDZK1 gene by homologous recombination. Kocher, O., Pal, R., Roberts, M., Cirovic, C., Gilchrist, A. Mol. Cell. Biol. (2003) [Pubmed]
  2. The membrane-associated protein pKe#192/MAP17 in human keratinocytes. Jaeger, C., Schaefer, B.M., Wallich, R., Kramer, M.D. J. Invest. Dermatol. (2000) [Pubmed]
  3. MAP17 overexpression is a common characteristic of carcinomas. Guijarro, M.V., Leal, J.F., Fominaya, J., Blanco-Aparicio, C., Alonso, S., Lleonart, M., Castellvi, J., Ruiz, L., Ramon Y Cajal, S., Carnero, A. Carcinogenesis (2007) [Pubmed]
  4. Transcriptional regulation of the SCL locus: identification of an enhancer that targets the primitive erythroid lineage in vivo. Delabesse, E., Ogilvy, S., Chapman, M.A., Piltz, S.G., Gottgens, B., Green, A.R. Mol. Cell. Biol. (2005) [Pubmed]
  5. Transcriptional regulation of the stem cell leukemia gene (SCL)--comparative analysis of five vertebrate SCL loci. Göttgens, B., Barton, L.M., Chapman, M.A., Sinclair, A.M., Knudsen, B., Grafham, D., Gilbert, J.G., Rogers, J., Bentley, D.R., Green, A.R. Genome Res. (2002) [Pubmed]
  6. Identification and partial characterization of a novel membrane-associated protein (MAP17) up-regulated in human carcinomas and modulating cell replication and tumor growth. Kocher, O., Cheresh, P., Lee, S.W. Am. J. Pathol. (1996) [Pubmed]
  7. Interaction of MAP17 with NHERF3/4 induces translocation of the renal Na/Pi IIa transporter to the trans-Golgi. Lanaspa, M.A., Giral, H., Breusegem, S.Y., Halaihel, N., Baile, G., Catal??n, J., Carrodeguas, J.A., Barry, N.P., Levi, M., Sorribas, V. Am. J. Physiol. Renal Physiol. (2007) [Pubmed]
  8. Identification and partial characterization of PDZK1: a novel protein containing PDZ interaction domains. Kocher, O., Comella, N., Tognazzi, K., Brown, L.F. Lab. Invest. (1998) [Pubmed]
  9. Rat kidney MAP17 induces cotransport of Na-mannose and Na-glucose in Xenopus laevis oocytes. Blasco, T., Aramayona, J.J., Alcalde, A.I., Catalán, J., Sarasa, M., Sorribas, V. Am. J. Physiol. Renal Physiol. (2003) [Pubmed]
  10. Structure of sperm activating protein. Leijonhufvud, P., Akerlöf, E., Pousette, A. Mol. Hum. Reprod. (1997) [Pubmed]
  11. Interactions of MAP17 with the NaPi-IIa/PDZK1 protein complex in renal proximal tubular cells. Pribanic, S., Gisler, S.M., Bacic, D., Madjdpour, C., Hernando, N., Sorribas, V., Gantenbein, A., Biber, J., Murer, H. Am. J. Physiol. Renal Physiol. (2003) [Pubmed]
  12. Identification of small PDZK1-associated protein, DD96/MAP17, as a regulator of PDZK1 and plasma high density lipoprotein levels. Silver, D.L., Wang, N., Vogel, S. J. Biol. Chem. (2003) [Pubmed]
  13. PDZK1, a novel PDZ domain-containing protein up-regulated in carcinomas and mapped to chromosome 1q21, interacts with cMOAT (MRP2), the multidrug resistance-associated protein. Kocher, O., Comella, N., Gilchrist, A., Pal, R., Tognazzi, K., Brown, L.F., Knoll, J.H. Lab. Invest. (1999) [Pubmed]
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