Genomes and Genes
A J Baines
Affiliation: University of Kent
- Evolution of the spectrin-based membrane skeletonA J Baines
School of Biosciences and Centre for Biomedical Informatics, University of Kent, CT2 7NJ, Canterbury, United Kingdom
Transfus Clin Biol 17:95-103. 2010..The spectrin/ankyrin/adducin/4.1 complex represents a remarkable system that underpins animal life; it has been adapted to many different functions at different times during animal evolution...
- A FERM-adjacent (FA) region defines a subset of the 4.1 superfamily and is a potential regulator of FERM domain functionAnthony J Baines
Department of Biosciences, University of Kent, Canterbury, CT2 7NJ, UK
BMC Genomics 7:85. 2006..In protein 4.1R, phosphorylation adjacent to the FERM domain regulates its activity, and membrane mechanical properties...
- The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteinsAnthony J Baines
Department of Biosciences, University of Kent, Canterbury, Kent, United Kingdom
Mol Biol Evol 26:2005-14. 2009..Overexpression of the CKK domain in PC12 cells blocked production of neurites, a process that requires microtubule function. We conclude that the CKK domain binds microtubules and represents a domain that evolved with the metazoa...
- Evolution of spectrin function in cytoskeletal and membrane networksAnthony J Baines
Department of Biosciences and Centre for Biomedical Informatics, University of Kent, Canterbury, Kent CT2 7NJ, UK
Biochem Soc Trans 37:796-803. 2009..I hypothesize that the elasticity of mammalian non-nucleated erythrocytes depends on the dynamic rearrangement of spectrin dimers/tetramers under the shearing forces experienced in circulation...
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal lifeAnthony J Baines
School of Biosciences and Centre for Biomedical Informatics, University of Kent, Canterbury, CT2 7NJ, UK
Protoplasma 244:99-131. 2010..The spectrin-ankyrin-4.1-adducin complex represents a remarkable system that underpins animal life; it has been adapted to many different functions at different times during animal evolution...
- The postsynaptic spectrin/4.1 membrane protein "accumulation machine"A J Baines
Department of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK
Cell Mol Biol Lett 6:691-702. 2001..By linking these receptors to the cytoskeletal and cell adhesion molecules that specify glutamatergic synapses, the membrane protein accumulation machine is suggested to direct the formation of postsynaptic signalling complexes...
- Properties of the C-terminal domain of 4.1 proteinsC Scott
Department of Biosciences, University of Kent, Canterbury, Kent, UK
Eur J Biochem 268:3709-17. 2001..Together these data indicate that the CTD probably represents an independent folding structure which has gained function since the divergence of vertebrates from invertebrates...
- Phosphorylation of a threonine unique to the short C-terminal isoform of betaII-spectrin links regulation of alpha-beta spectrin interaction to neuritogenesisPaola A Bignone
Department of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, Great Britain
J Biol Chem 282:888-96. 2007..Furthermore, because both the T2159E mutant and the wild-type allow neuritogenesis, we conclude that the short C-terminal betaII-spectrin is phosphorylated during this process...
- Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activitiesN V Hayes
Department of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, England
J Cell Sci 113:2023-34. 2000..We conclude that variation in the structure of the C-terminal regions of betaII spectrin isoforms correlates with their differential intracellular targeting...
- Ca2+-dependent interaction with calmodulin is conserved in the synapsin family: identification of a high-affinity siteS Nicol
Research School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, England
Biochemistry 36:11487-95. 1997..We conclude that calmodulin binding to synapsins is likely to be a general aspect of regulation of synaptic function...
- Synapsin I and the cytoskeleton: calmodulin regulation of interactionsA J Baines
Research School of Biosciences, University of Kent, Canterbury, U.K
Biochem Soc Trans 23:65-70. 1995
- Identification and characterization of novel spliced variants of neuregulin 4 in prostate cancerNandini V L Hayes
Cancer Biology Laboratory, Research School of Biosciences, Centre for Biomedical Informatics, Institute of Mathematics and Statistics, University of Kent, Canterbury, UK
Clin Cancer Res 13:3147-55. 2007..The aims of this study were to establish whether the fourth member of this family, NRG4, is expressed in prostate cancer, if it is alternatively spliced and whether any functional differences between the variants could be observed...
- Characterization of the cell membrane-associated products of the Neuregulin 4 geneN V L Hayes
Cancer Biology Laboratory, Research School of Biosciences, University of Kent, Canterbury, UK
Oncogene 27:715-20. 2008....
- Protein 4.1 and the control of ion channelsAnthony J Baines
Department of Biosciences, University of Kent, Canterbury, CT2 7NJ Kent, UK
Blood Cells Mol Dis 42:211-5. 2009..A hypothesis to investigate in the future is that differential regulation of 4.1 and ankyrins (e.g. by PIP(2)) allows highly selective control of cell surface accumulation and transport activity of a specific range of ion channels...
- Site specificity in the interactions of synapsin 1 with tubulinA F Bennett
Biological Laboratory, University of Kent, Canterbury, U K
Biochem J 276:793-9. 1991..Our results show that there are tubulin-binding sites in both head and tail domains. We conclude that synapsin 1 monomers should be able to cross-link microtubules...
- Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization sitePaola A Bignone
Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK
Biochem J 374:613-24. 2003....
- Protein engineering of the 2-haloacid halidohydrolase IVa from Pseudomonas cepacia MBA4W Asmara
International Institute of Biotechnology, University of Kent, Canterbury, U K
Biochem J 292:69-74. 1993....
- The spectrin-associated cytoskeleton in mammalian heartAnthony J Baines
Department of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK
Front Biosci 10:3020-33. 2005....
- Predicting post-synaptic activity in proteins with data miningGisele L Pappa
Computing Laboratory, University of Kent, Canterbury, UK
Bioinformatics 21:ii19-25. 2005..The discovered rules were analysed with respect to their predictive accuracy (generalization ability) and with respect to their interestingness to biologists (in the sense of representing novel, unexpected knowledge)...
- Comprehensive analysis of all triple helical repeats in beta-spectrins reveals patterns of selective evolutionary conservationAnthony J Baines
Randall Centre for Molecular Mechanisms of Cell Function, King s College London, Guy s Campus, UK
Cell Mol Biol Lett 8:195-214. 2003....
- Expression of human membrane skeleton protein genes for protein 4.1 and betaIISigma2-spectrin assayed by real-time RT-PCRPamela M Taylor-Harris
Randall Division of Cell and Molecular Biophysics, King's College London, Guy's Campus, London SE1 1UL, UK
Cell Mol Biol Lett 10:135-49. 2005..4.1R abundance was very low in both tissues. Whilst we expected that 4.1 mRNAs would feature highly in muscle and nerve, we note their high abundance in testis, indicating previously unsuspected functions in reproduction...
- Cardiac muscle cell cytoskeletal protein 4.1: analysis of transcripts and subcellular location--relevance to membrane integrity, microstructure, and possible role in heart failurePamela M Taylor-Harris
Randall Division of Cell and Molecular Biophysics, King s College London, Guy s Campus, London SE1 1UL, UK
Mamm Genome 16:137-51. 2005..We speculate that over the repetitive cycles of heart muscle contraction and relaxation, 4.1s are likely to locate, support, and coordinate functioning of key membrane-bound macromolecular assemblies...
- Molecular evolution of ankyrin: gain of function in vertebrates by acquisition of an obscurin/titin-binding-related domainAlexander A Hopitzan
, Paris, France
Mol Biol Evol 23:46-55. 2006..We suggest that the OTBD represents an adaptation of the cytoskeleton that confers muscle cells with resilience to the forces associated with vertebrate life...
- Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteinsXiuli An
Red Cell Physiology Laboratory, New York Blood Center, 310 East 67th Street, New York, New York 10021, USA
Biochemistry 45:5725-32. 2006..1R, 4.1B, 4.1G, and 4.1N) are widely expressed and the PIP2-binding motifs are highly conserved, it is likely that the functions of other 4.1 proteins are similarly regulated by PIP2 in many different cell types...
- Conformational stabilities of the structural repeats of erythroid spectrin and their functional implicationsXiuli An
Red Cell Physiology Laboratory, New York Blood Center, 310 E 67th Street, New York, NY 10021, USA
J Biol Chem 281:10527-32. 2006....
- Thermal stabilities of brain spectrin and the constituent repeats of subunitsXiuli An
Red Cell Physiology Laboratory, New York Blood Center, New York, New York 10021, USA
Biochemistry 45:13670-6. 2006..The greater structural stability of the repeats in alphaII- and betaII-spectrin may account, at least in part, for the higher rigidity of brain compared to erythrocyte spectrin...
- The transitional junction: a new functional subcellular domain at the intercalated discPauline M Bennett
Randall Division of Cell and Molecular Biophysics, GKT School of Biomedical Sciences, King s College London, Guy s Campus, London SE1 1UL, United Kingdom
Mol Biol Cell 17:2091-100. 2006..In particular, it provides a means for sarcomeres to be added to the ends of the cells during growth. This is of particular relevance to understanding myocyte elongation in dilated cardiomyopathy...
- Distinct distribution of specific members of protein 4.1 gene family in the mouse nephronMohamed Ramez
Department of Subcellular Structure, Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
Kidney Int 63:1321-37. 2003..1G in kidney. CONCLUSION: Distinct distribution of 4.1 proteins along the nephron suggests their involvement in targeting of selected transmembrane proteins in kidney epithelium and, therefore, in regulation of specific kidney functions...
- Mammalian alpha I-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytesMarcela Salomao
Red Cell Physiology Laboratory, New York Blood Center, New York, NY 10021, USA
Proc Natl Acad Sci U S A 103:643-8. 2006..We conclude that alphaI-spectrin represents a neofunctionalized spectrin adapted to the rapid make and break of tetramers...
- Ankyrin-G in skeletal muscle: tissue-specific alternative splicing contributes to the complexity of the sarcolemmal cytoskeletonAlexander A Hopitzan
Institut Jacques Monod CNRS Universités Paris VI et VII 2 Place Jussieu, F 75251 Paris Cedex 05, France
Exp Cell Res 309:86-98. 2005..Our results demonstrate the tissue-dependent alternative splicing of Ank3 in skeletal muscle and point to novel functions of small ankyrins-G in organizing microdomains of the plasma membrane...