Abstract
Chicken drebrin isoforms were first identified in the optic tectum of developing brain. Although the time course of protein expression was different in each drebrin isoform, the similarity between their protein structures was suggested by biochemical analysis of purified protein. To determine their protein structures, the cloning of drebrin cDNAs was conducted. Comparison between the cDNA sequences shows that all drebrin cDNAs are identical except that the internal insertion sequences are present or absent in their sequences. Chicken drebrin are now classified into three isoforms, namely, drebrins E1, E2, and A. Genomic cloning demonstrated that the three isoforms are generated by an alternative splicing of individual exons encoding the insertion sequences from single drebrin gene. The mechanism should be precisely regulated in cell-type-specific and developmental stage-specific fashion. Drebrin protein, which is well conserved in various vertebrate species, although mammalian drebrin has only two isoforms, namely, drebrin E and drebrin A, is different from chicken drebrin that has three isoforms. Drebrin belongs to an actin-depolymerizing factor homology (ADF-H) domain protein family. Besides the ADF-H domain, drebrin has other domains, including the actin-binding domain and Homer-binding motifs. Diversity of protein isoform and multiple domains of drebrin could interact differentially with the actin cytoskeleton and other intracellular proteins and regulate diverse cellular processes.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsNotes
- 1.
Exon 12 was referred to as exon 11 in the original reports published before the discovery of the initial (5’ terminal) exon (Jin et al. 2003; Kojima et al. 2010).
References
Aoki C et al (2005) Drebrin A is a postsynaptic protein that localizes in vivo to the submembranous surface of dendritic sites forming excitatory synapses. J Comp Neurol 483:383–402
Drubin DG et al (1988) Yeast actin-binding proteins: evidence for a role in morphogenesis. J Cell Biol 107(Pt 2):2551–2561
Grintsevich EE et al (2010) Mapping of drebrin binding site on F-actin. J Mol Biol 398:542–554
Hayashi K et al (1999) Domain analysis of the actin-binding and actin-remodeling activities of drebrin. Exp Cell Res 253:673–680
Ishikawa R et al (1994) Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J Biol Chem 269:29928–29933
Jin M et al (2002) A novel, brain-specific mouse drebrin: cDNA cloning, chromosomal mapping, genomic structure, expression, and functional characterization. Genomics 79:686–692
Keon BH et al (2000) Isoform specific expression of the neuronal F-actin binding protein, drebrin, in specialized cells of stomach and kidney epithelia. J Cell Sci 113(Pt 2):325–336
Kessels MM, Engqvist-Goldstein AEY, Drubin DG (2000) Association of Mouse Actin-binding Protein 1 (mAbp1/SH3P7), an Src Kinase Target, with Dynamic Regions of the Cortical Actin Cytoskeleton in Response to Rac1 Activation. Mol Biol Cell 11:393–412
Kojima N et al (1988) Nucleotide sequences of two embryonic drebrins, developmentally regulated brain proteins, and developmental change in their mRNAs. Brain Res 464:207–215
Kojima N et al (1993) Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene. Brain Res Mol Brain Res 19:101–114
Kojima N et al (2010) Genetic disruption of the alternative splicing of drebrin gene impairs context-dependent fear learning in adulthood. Neuroscience 165:138–150
Kojima N et al (2016) Drebrin A regulates hippocampal LTP and hippocampus-dependent fear learning in adult mice. Neuroscience 324:218–226
Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105–132
Lappalainen P et al (1998) The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol Biol Cell 9:1951–1959
Luna EJ, Pestonjamasp KN, Cheney RE, Strassel CP, Lu TH, Chia CP, Hitt AL, Fechheimer M, Furthmayr H, Mooseker MS (1997) Actin-binding membrane proteins identified by F-actin blot overlays. Soc Gen Physiol Ser 52:3–18
Mammoto A et al (1998) Interactions of drebrin and gephyrin with profilin. Biochem Biophys Res Commun 243:86–89
Peitsch WK, Grund C, Kuhn C, Schnölzer M, Spring H, Schmelz M, Franke WW (1999) Drebrin is a widespread actin-associating protein enriched at junctional plaques, defining a specific microfilament anchorage system in polar epithelial cells. Eur J Cell Biol 78:767–778
Poukkula M et al (2011) Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics. Cytoskeleton 68:471–490
Roy B et al (2013) Review: alternative Splicing (AS) of genes as an approach for generating protein complexity. Curr Genomics 14:182–194
Sasaki Y, Hayashi K, Shirao T, Ishikawa R, Kohama K (1996) Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J Neurochem 66:980–988
Shirao T, Obata K (1985) Two acidic proteins associated with brain development in chick embryo. J Neurochem 44:1210–1216
Shirao T, Obata K (1986) Immunochemical homology of 3 developmentally regulated brain proteins and their developmental change in neuronal distribution. Brain Res 394:233–244
Shirao T, Inoue HK, Kano Y, Obata K (1987) Localization of a developmentally regulated neuron-specific protein S54 in dendrites as revealed by immunoelectron microscopy. Brain Res 413:374–378
Shirao T et al (1988) Molecular cloning of a cDNA for the developmentally regulated brain protein, drebrin. Brain Res 464:71–74
Shirao T et al (1989) Two forms of drebrins, developmentally regulated brain proteins, in rat. Proceedings of the Japan Academy 65:169–172
Shirao T et al (1990) Expression of three drebrin isoforms in the developing nervous system. Neurosci Res Suppl 13:S106–S111
Shirao T et al (1992) Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. Neuroreport 3:109–112
Shirao T, Hayashi K, Ishikawa R, Isa K, Asada H, Ikeda K, Uyemura K (1994) Formation of thick, curving bundles of actin by drebrin A expressed in fibroblasts. Exp Cell Res 215:145–153
Song M et al (2008) Expression of drebrin E in migrating neuroblasts in adult rat brain: coincidence between drebrin E disappearance from cell body and cessation of migration. Neuroscience 152:670–682
Sparks AB et al (1996) Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins. Nat Biotechnol 14:741–744
Toda M et al (1993) Molecular cloning of cDNA encoding human drebrin E and chromosomal mapping of its gene. Biochem Biophys Res Commun 196:468–472
Tu JC et al (1998) Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors. Neuron 21:717–726
Yamazaki H et al (2001) Molecular cloning and dendritic localization of rat SH3P7. Eur J Neurosci 14:998–1008
Yamazaki H et al (2014) Spikar, a novel drebrin-binding protein, regulates the formation and stabilization of dendritic spines. J Neurochem 128:507–522
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2017 Springer Japan KK
About this chapter
Cite this chapter
Kojima, N. (2017). Molecular Cloning of Drebrin: Progress and Perspectives. In: Shirao, T., Sekino, Y. (eds) Drebrin. Advances in Experimental Medicine and Biology, vol 1006. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56550-5_2
Download citation
DOI: https://doi.org/10.1007/978-4-431-56550-5_2
Published:
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-56548-2
Online ISBN: 978-4-431-56550-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)