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Gene Review

kel  -  kelch

Drosophila melanogaster

Synonyms: CG7210, Dm.Ring_canal/KELC_DROME, Dmel\CG7210, Kel, Kelch, ...
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Disease relevance of kel

  • The only detected defect for kelch mutants is female sterility, and kelch protein is localized to the ovarian ring canals. kelch mutant ring canals are disorganized and have partly occluded lumens, causing a failure to transport cytoplasm [1].
  • Although the protein sequence of scruin has no homology to any known actin-binding protein, it has similarities to several proteins, including four open reading frames of unknown function in poxviruses, as well as kelch, a Drosophila protein localized to actin-rich ring canals [2].

High impact information on kel

  • Oocyte maturation in Drosophila is supported by a cluster of 15 germline-derived nurse cells whose cytoplasm is transported into the oocyte through intercellular bridges called ring canals. kelch was isolated as a female sterile mutation affecting cytoplasm transport [3].
  • We have cloned the kelch gene and found that it encodes an unusual transcript containing two open reading frames (ORF1 and ORF2) separated by a single UGA stop codon [3].
  • The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to the actin-associated proteins kelch and scruin [4].
  • Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation [5].
  • Two-dimensional electrophoresis demonstrated that Kelch is tyrosine phosphorylated in a src64-dependent pathway [5].

Biological context of kel


Anatomical context of kel

  • In imp-alpha2(D14) the transfer of nurse cell components to the oocyte is interrupted and the Kelch protein, an oligomeric ring canal actin organizer, is normally produced but fails to associate with the ring canals resulting in their occlusion [8].
  • Oligomerization through the amino half of kelch might allow cross-linking of ring canal actin filaments, organizing the inner rim cytoskeleton [9].
  • Transient induction of ENC-1, a Kelch-related actin-binding protein, is required for adipocyte differentiation [10].

Associations of kel with chemical compounds

  • The known ring canal proteins, phosphotyrosine-containing protein(s), F-actin, hts- and kelch proteins, are localized to the inner rim at a later developmental time [11].

Other interactions of kel

  • Immunohistochemistry shows that, although the Imp-alpha2 protein cannot be detected on the ring canals, the Kelch protein, a known ring canal component, fails to bind to ring canals in imp-alpha 2(D14) egg chambers [6].
  • Two mutations, hu-li tai shao (hts) and kelch, disrupt normal ring canal development [12].
  • We also recovered as maternal-effect mutations four dl alleles, as well as six alleles of quail and one allele of kelch, two previously identified maternal-effect genes [13].
  • Mayven contains a BTB (broad complex, tramtrack, bric-a-brac)/POZ (poxvirus, zinc finger) domain-like structure in the predicted N terminus and "kelch repeats" in the predicted C-terminal domain [14].

Analytical, diagnostic and therapeutic context of kel


  1. Examination of the function of two kelch proteins generated by stop codon suppression. Robinson, D.N., Cooley, L. Development (1997) [Pubmed]
  2. Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm. Way, M., Sanders, M., Garcia, C., Sakai, J., Matsudaira, P. J. Cell Biol. (1995) [Pubmed]
  3. kelch encodes a component of intercellular bridges in Drosophila egg chambers. Xue, F., Cooley, L. Cell (1993) [Pubmed]
  4. The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to the actin-associated proteins kelch and scruin. Varkey, J.P., Muhlrad, P.J., Minniti, A.N., Do, B., Ward, S. Genes Dev. (1995) [Pubmed]
  5. Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation. Kelso, R.J., Hudson, A.M., Cooley, L. J. Cell Biol. (2002) [Pubmed]
  6. Importin-alpha 2 is critically required for the assembly of ring canals during Drosophila oogenesis. Gorjánácz, M., Adám, G., Török, I., Mechler, B.M., Szlanka, T., Kiss, I. Dev. Biol. (2002) [Pubmed]
  7. Soma-to-germline interactions during Drosophila oogenesis are influenced by dose-sensitive interactions between cut and the genes cappuccino, ovarian tumor and agnostic. Jackson, S.M., Berg, C.A. Genetics (1999) [Pubmed]
  8. Domains of Importin-alpha2 required for ring canal assembly during Drosophila oogenesis. Gorjánácz, M., Török, I., Pomozi, I., Garab, G., Szlanka, T., Kiss, I., Mechler, B.M. J. Struct. Biol. (2006) [Pubmed]
  9. Drosophila kelch is an oligomeric ring canal actin organizer. Robinson, D.N., Cooley, L. J. Cell Biol. (1997) [Pubmed]
  10. Transient induction of ENC-1, a Kelch-related actin-binding protein, is required for adipocyte differentiation. Zhao, L., Gregoire, F., Sul, H.S. J. Biol. Chem. (2000) [Pubmed]
  11. Mucinoprotein is a universal constituent of stable intercellular bridges in Drosophila melanogaster germ line and somatic cells. Kramerova, I.A., Kramerov, A.A. Dev. Dyn. (1999) [Pubmed]
  12. Morphogenesis of Drosophila ovarian ring canals. Robinson, D.N., Cant, K., Cooley, L. Development (1994) [Pubmed]
  13. The genetics of the dorsal-Bicaudal-D region of Drosophila melanogaster. Steward, R., Nüsslein-Volhard, C. Genetics (1986) [Pubmed]
  14. Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain. Soltysik-Espanola, M., Rogers, R.A., Jiang, S., Kim, T.A., Gaedigk, R., White, R.A., Avraham, H., Avraham, S. Mol. Biol. Cell (1999) [Pubmed]
  15. Molecular phylogeny of the kelch-repeat superfamily reveals an expansion of BTB/kelch proteins in animals. Prag, S., Adams, J.C. BMC Bioinformatics (2003) [Pubmed]
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