Derek Blake

Last updated February 07, 2022

Derek Blake was, until 2007, the Isobel Laing Post-Doctoral Fellow in Biomedical Sciences, and the Wellcome Trust Senior Fellow in Basic Biomedical Science, Oriel College, Oxford.^[1]

He holds a doctorate (D.Phil.) and a Bachelor's (B.Sc. from Liverpool). Blake graduated in Biochemistry and worked on his D.Phil. studies in the Sir William Dunn School of Pathology, Oxford, taking post-doctoral research on the molecular basis of muscular dystrophy.

His research interests lie in the molecular basis of neuronal dysfunction in patients with Duchenne muscular dystrophy and congenital muscular dystrophies (CMD). This led to the discovery of components of the dystrophin protein complex in neurons and identified new genes and pathways that are involved in the pathogenesis of CMD. He was awarded a Wellcome Trust Career Development Fellowship in 1996 and a Wellcome Trust Senior Fellowship in Basic Biomedical Science in 2000. Blake is a member of the American Society for Cell Biology and an editor of the Journal of Nanobiotechnology. Blake's research interests include molecular aspects of neuronal function in muscular dystrophies, glycosyltransferases in neurons and muscle cells, the neuromuscular junction and molecular architecture of the sarcolemma.

Publications

Blake D.J., Hawkes R., Benson M.A. and Beesley P. (1999) Different dystrophin-like complexes are found in neurons and glia. J. Cell Biol. 147: 645-657.
Blake D.J. and Kröger S. (2000) The molecular neurobiology of muscular dystrophy: Learning lessons from muscle? Trends Neurosci. 23: 92-99.
Newey S.E., Benson, M.A., Ponting C.P., Davies K.E. and Blake D.J. (2000) Alternative splicing of dystrobrevin regulates the stoichiometry of syntrophin binding to the dystrophin protein complex. Curr. Biol. 10: 12951298.
Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R. and Blake D.J. (2001) Dysbindin, a novel coiled-coil containing protein that interacts with the dystrobrevins in muscle and brain. J. Biol. Chem. 276: 24232-24241.
Brockington M., Blake D. J., Prandini P., Brown S. C., Torelli S., Benson M. A., Ponting C. P., Estournet B., Romero N. B., Mercuri E., Voit T., Sewry C. A., Guicheney P. and Muntoni F. (2001) Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin a2 deficiency and abnormal glycosylation of a-dystroglycan. Am J. Hum. Genet. 69: 1198-1209.
Brockington M., Yuva Y., Prandini P., Brown S. C., Torelli S., Benson M. A., Herrmann R., Anderson L. V. B., Bashir R., Burgunder J-M., Fallet S., Romero, N., Guicheney P., Fardeau M., Straub V., Reynolds G., Pollitt C., Sewry C. A., Bushby K., Voit T., Blake D. J. and Muntoni F. (2001) Mutations in the Fukutin Related-Protein gene (FKRP) identifies Limb Girdle Muscular Dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C. Hum. Mol. Genet. 10: 2851-2859.
Blake D. J, Weir A., Newey S. E. and Davies K. E. (2002) Function and genetics of dystrophin and dystrophin-related proteins in muscle. Phys. Rev. 82: 291-329.

Related Research Articles

Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC). Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere. It has a molecular weight of 427 kDa

Utrophin is a protein that in humans is encoded by the UTRN gene.

Syncoilin is a muscle-specific atypical type III intermediate filament protein encoded in the human by the gene SYNC. It was first isolated as a binding partner to α-dystrobrevin, as determined by a yeast two-hybrid assay.

Dystrobrevin is a protein that binds to dystrophin in the costamere of skeletal muscle cells. In humans, there are at least two isoforms of dystrobrevin, dystrobrevin alpha and dystrobrevin beta.

Fukutin is a eukaryotic protein necessary for the maintenance of muscle integrity, cortical histogenesis, and normal ocular development. Mutations in the fukutin gene have been shown to result in Fukuyama congenital muscular dystrophy (FCMD) characterised by brain malformation - one of the most common autosomal-recessive disorders in Japan. In humans this protein is encoded by the FCMD gene, located on chromosome 9q31. Human fukutin exhibits a length of 461 amino acids and a predicted molecular mass of 53.7 kDa.

Fukutin-related protein (FKRP) is a protein associated with congenital muscular dystrophy.

Micropolygyria, is a neuronal migration disorder, a developmental anomaly of the brain characterized by development of numerous small convolutions (microgyri), causing intellectual disability and/or other neurological disorders. It is present in a number of specific neurological diseases, notably multiple sclerosis and Fukuyama congenital muscular dystrophy, a specific disease cause by mutation in the Fukutin gene (FKTN).

Alpha-1-syntrophin is a protein that in humans is encoded by the SNTA1 gene. Alpha-1 syntrophin is a signal transducing adaptor protein and serves as a scaffold for various signaling molecules. Alpha-1 syntrophin contains a PDZ domain, two Pleckstrin homology domain and a 'syntrophin unique' domain.

Alpha-7 integrin is a protein that in humans is encoded by the ITGA7 gene. Alpha-7 integrin is critical for modulating cell-matrix interactions. Alpha-7 integrin is highly expressed in cardiac muscle, skeletal muscle and smooth muscle cells, and localizes to Z-disc and costamere structures. Mutations in ITGA7 have been associated with congenital myopathies and noncompaction cardiomyopathy, and altered expression levels of alpha-7 integrin have been identified in various forms of muscular dystrophy.

Beta-sarcoglycan is a protein that in humans is encoded by the SGCB gene.

Delta-sarcoglycan is a protein that in humans is encoded by the SGCD gene.

Beta-2-syntrophin is a protein that in humans is encoded by the SNTB2 gene.

Alpha-sarcoglycan is a protein that in humans is encoded by the SGCA gene.

Beta-1-syntrophin is a protein that in humans is encoded by the SNTB1 gene.

Selenoprotein N is a protein that in humans is encoded by the SEPN1 gene.

Glycosyltransferase-like protein LARGE1 is an enzyme that in humans is encoded by the LARGE gene.

Dystrobrevin alpha is a protein that in humans is encoded by the DTNA gene.

Dystrobrevin beta is a protein which in humans is encoded by the DTNB gene.

Collagen VI (ColVI) is a type of collagen primarily associated with the extracellular matrix of skeletal muscle. ColVI maintains regularity in muscle function and stabilizes the cell membrane. It is synthesized by a complex, multistep pathway that leads to the formation of a unique network of linked microfilaments located in the extracellular matrix (ECM). ColVI plays a vital role in numerous cell types, including chondrocytes, neurons, myocytes, fibroblasts, and cardiomyocytes. ColVI molecules are made up of three alpha chains: α1(VI), α2(VI), and α3(VI). It is encoded by 6 genes: COL6A1, COL6A2, COL6A3, COL6A4, COL6A5, and COL6A6. The chain lengths of α1(VI) and α2(VI) are about 1,000 amino acids. The chain length of α3(VI) is roughly a third larger than those of α1(VI) and α2(VI), and it consists of several spliced variants within the range of 2,500 to 3,100 amino acids.

Chaperone-assisted selective autophagy is a cellular process for the selective, ubiquitin-dependent degradation of chaperone-bound proteins in lysosomes.

References

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