Functional and genetic analysis of spectraplakins in DrosophilaCitation formats

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Functional and genetic analysis of spectraplakins in Drosophila. / Hahn, Ines; Ronshaugen, Matthew; Sanchez-Soriano, Natalia; Prokop, Andreas.

Methods in Enzymology: Intermediate Filament Associated Proteins. ed. / Katherine L. Wilson; Arnoud Sonnenberg. Vol. 569 Elsevier BV, 2016. p. 373-405 (Methods in Enzymology; Vol. 569).

Research output: Chapter in Book/Report/Conference proceedingChapter

Harvard

Hahn, I, Ronshaugen, M, Sanchez-Soriano, N & Prokop, A 2016, Functional and genetic analysis of spectraplakins in Drosophila. in KL Wilson & A Sonnenberg (eds), Methods in Enzymology: Intermediate Filament Associated Proteins. vol. 569, Methods in Enzymology, vol. 569, Elsevier BV, pp. 373-405. https://doi.org/10.1016/bs.mie.2015.06.022

APA

Hahn, I., Ronshaugen, M., Sanchez-Soriano, N., & Prokop, A. (2016). Functional and genetic analysis of spectraplakins in Drosophila. In K. L. Wilson, & A. Sonnenberg (Eds.), Methods in Enzymology: Intermediate Filament Associated Proteins (Vol. 569, pp. 373-405). (Methods in Enzymology; Vol. 569). Elsevier BV. https://doi.org/10.1016/bs.mie.2015.06.022

Vancouver

Hahn I, Ronshaugen M, Sanchez-Soriano N, Prokop A. Functional and genetic analysis of spectraplakins in Drosophila. In Wilson KL, Sonnenberg A, editors, Methods in Enzymology: Intermediate Filament Associated Proteins. Vol. 569. Elsevier BV. 2016. p. 373-405. (Methods in Enzymology). https://doi.org/10.1016/bs.mie.2015.06.022

Author

Hahn, Ines ; Ronshaugen, Matthew ; Sanchez-Soriano, Natalia ; Prokop, Andreas. / Functional and genetic analysis of spectraplakins in Drosophila. Methods in Enzymology: Intermediate Filament Associated Proteins. editor / Katherine L. Wilson ; Arnoud Sonnenberg. Vol. 569 Elsevier BV, 2016. pp. 373-405 (Methods in Enzymology).

Bibtex

@inbook{cfa97ade12be4b96b73b295ac5fc291e,
title = "Functional and genetic analysis of spectraplakins in Drosophila",
abstract = "The cytoskeleton is a dynamic network of filamentous protein polymers required for virtually all cellular processes. It consists of three major classes, filamentous actin (F-actin), intermediate filaments and microtubules, all displaying characteristic structural properties, functions, cellular distributions and sets of interacting regulatory proteins. One unique class of proteins, the spectraplakins, bind, regulate, and integrate the functions of all three classes of cytoskeleton proteins. Spectraplakins are giant, evolutionary conserved multidomain proteins (spanning up to 9000 aa) that are true members of the plakin, spectrin and Gas2-like protein families. They have OMIM-listed disease links to epidermolysis bullosa and hereditary sensory and autonomic neuropathy (HSAN). Their role in disease is likely underrepresented since studies in model animal systems have revealed critical roles in polarity, morphogenesis, differentiation and maintenance, migration, signalling and intracellular trafficking in a variety of tissues. This enormous diversity of spectraplakin function is consistent with the numerous isoforms produced from single genomic loci that combine different sets of functional domains in distinct cellular contexts. To study the broad range of functions and complexity of these proteins, Drosophila is a powerful model. Thus, the fly spectraplakin Short stop (Shot) acts as an actin-microtubule linker and plays important roles in many developmental processes, which provide experimentally amenable and relevant contexts in which to study spectraplakin functions. For these studies, a versatile range of relevant experimental resources that facilitate genetics and transgenic approaches, highly refined genomics tools, and an impressive set of spectraplakin-specific genetic and molecular tools is readily available. Here we use the example of Shot to illustrate how the various tools and strategies available for Drosophila can be employed to decipher and dissect cellular roles and molecular mechanisms of spectraplakins.",
keywords = "Drosophila, spectraplakins, cytoskeleton, actin, microtubules, FlyBase, methods, techniques",
author = "Ines Hahn and Matthew Ronshaugen and Natalia Sanchez-Soriano and Andreas Prokop",
note = "All authors were supported by the Biotechnology and Biological Sciences Research Council (BBSRC), in particular A.P., N.S.S. and I.H. by the project grants BB/L000717/1 and BB/I002448/1, and M.R. through BB/H017801/1.",
year = "2016",
doi = "10.1016/bs.mie.2015.06.022",
language = "English",
isbn = "9780128034699",
volume = "569",
series = "Methods in Enzymology",
publisher = "Elsevier BV",
pages = "373--405",
editor = "Wilson, {Katherine L. } and Arnoud Sonnenberg",
booktitle = "Methods in Enzymology",
address = "Netherlands",

}

RIS

TY - CHAP

T1 - Functional and genetic analysis of spectraplakins in Drosophila

AU - Hahn, Ines

AU - Ronshaugen, Matthew

AU - Sanchez-Soriano, Natalia

AU - Prokop, Andreas

N1 - All authors were supported by the Biotechnology and Biological Sciences Research Council (BBSRC), in particular A.P., N.S.S. and I.H. by the project grants BB/L000717/1 and BB/I002448/1, and M.R. through BB/H017801/1.

PY - 2016

Y1 - 2016

N2 - The cytoskeleton is a dynamic network of filamentous protein polymers required for virtually all cellular processes. It consists of three major classes, filamentous actin (F-actin), intermediate filaments and microtubules, all displaying characteristic structural properties, functions, cellular distributions and sets of interacting regulatory proteins. One unique class of proteins, the spectraplakins, bind, regulate, and integrate the functions of all three classes of cytoskeleton proteins. Spectraplakins are giant, evolutionary conserved multidomain proteins (spanning up to 9000 aa) that are true members of the plakin, spectrin and Gas2-like protein families. They have OMIM-listed disease links to epidermolysis bullosa and hereditary sensory and autonomic neuropathy (HSAN). Their role in disease is likely underrepresented since studies in model animal systems have revealed critical roles in polarity, morphogenesis, differentiation and maintenance, migration, signalling and intracellular trafficking in a variety of tissues. This enormous diversity of spectraplakin function is consistent with the numerous isoforms produced from single genomic loci that combine different sets of functional domains in distinct cellular contexts. To study the broad range of functions and complexity of these proteins, Drosophila is a powerful model. Thus, the fly spectraplakin Short stop (Shot) acts as an actin-microtubule linker and plays important roles in many developmental processes, which provide experimentally amenable and relevant contexts in which to study spectraplakin functions. For these studies, a versatile range of relevant experimental resources that facilitate genetics and transgenic approaches, highly refined genomics tools, and an impressive set of spectraplakin-specific genetic and molecular tools is readily available. Here we use the example of Shot to illustrate how the various tools and strategies available for Drosophila can be employed to decipher and dissect cellular roles and molecular mechanisms of spectraplakins.

AB - The cytoskeleton is a dynamic network of filamentous protein polymers required for virtually all cellular processes. It consists of three major classes, filamentous actin (F-actin), intermediate filaments and microtubules, all displaying characteristic structural properties, functions, cellular distributions and sets of interacting regulatory proteins. One unique class of proteins, the spectraplakins, bind, regulate, and integrate the functions of all three classes of cytoskeleton proteins. Spectraplakins are giant, evolutionary conserved multidomain proteins (spanning up to 9000 aa) that are true members of the plakin, spectrin and Gas2-like protein families. They have OMIM-listed disease links to epidermolysis bullosa and hereditary sensory and autonomic neuropathy (HSAN). Their role in disease is likely underrepresented since studies in model animal systems have revealed critical roles in polarity, morphogenesis, differentiation and maintenance, migration, signalling and intracellular trafficking in a variety of tissues. This enormous diversity of spectraplakin function is consistent with the numerous isoforms produced from single genomic loci that combine different sets of functional domains in distinct cellular contexts. To study the broad range of functions and complexity of these proteins, Drosophila is a powerful model. Thus, the fly spectraplakin Short stop (Shot) acts as an actin-microtubule linker and plays important roles in many developmental processes, which provide experimentally amenable and relevant contexts in which to study spectraplakin functions. For these studies, a versatile range of relevant experimental resources that facilitate genetics and transgenic approaches, highly refined genomics tools, and an impressive set of spectraplakin-specific genetic and molecular tools is readily available. Here we use the example of Shot to illustrate how the various tools and strategies available for Drosophila can be employed to decipher and dissect cellular roles and molecular mechanisms of spectraplakins.

KW - Drosophila, spectraplakins, cytoskeleton, actin, microtubules, FlyBase, methods, techniques

U2 - 10.1016/bs.mie.2015.06.022

DO - 10.1016/bs.mie.2015.06.022

M3 - Chapter

SN - 9780128034699

VL - 569

T3 - Methods in Enzymology

SP - 373

EP - 405

BT - Methods in Enzymology

A2 - Wilson, Katherine L.

A2 - Sonnenberg, Arnoud

PB - Elsevier BV

ER -