Spectrin, α-Actinin, and Dystrophin

Broderick, Mike; Winder, Steven J.

doi:10.1016/s0065-3233(05)70007-3

Cited by 120 publications

(127 citation statements)

References 219 publications

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“…The cytoskeleton is highly dynamic and has the ability to remodel itself quickly during normal developmental morphogenesis or upon tissue injury. Spectraplakins function in these remodeling processes through their unique ability to crosslink and integrate different cytoskeletal networks to regulate various cellular processes (Broderick and Winder, 2005;Liem, 2016;Röper et al, 2002). Spectraplakins are part of the spectrin superfamily and are large, evolutionarily conserved cytoskeletal proteins that can bind to different cytoskeletal networks to coordinate cytoskeletal dynamics (Broderick and Winder, 2005;Liem, 2016;Röper et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Zhang

Yue

2017

Journal of Cell Science

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The different cytoskeletal networks in a cell are responsible for many fundamental cellular processes. Current studies have shown that spectraplakins, cytoskeletal crosslinkers that combine features of both the spectrin and plakin families of crosslinkers, have a critical role in integrating these different cytoskeletal networks. Spectraplakin genes give rise to a variety of isoforms that have distinct functions. Importantly, all spectraplakin isoforms are uniquely able to associate with all three elements of the cytoskeleton, namely, F-actin, microtubules and intermediate filaments. In this Review, we will highlight recent studies that have unraveled their function in a wide range of different processes, from regulating cell adhesion in skin keratinocytes to neuronal cell migration. Taken together, this work has revealed a diverse and indispensable role for orchestrating the function of different cytoskeletal elements in vivo.

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Section: Introductionmentioning

confidence: 99%

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Zhang

Yue

2017

Journal of Cell Science

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“…(2) The spectrins (α-/ β-spectrin, α-actinin, dystrophin, and utrophin) are highly conserved actinlinked scaffolding proteins primarily at the cell cortex which form essential links between membrane and cytoplasmic proteins (Broderick & Winder, 2005;Machnicka et al, 2014). (3) The Gas2-like proteins (Gas2, Gas2-like 1-3) act as linkers between MTs, end-binding (EB) proteins, and F-actin, important for cytoskeletal dynamics in cell division and development (Sharaby et al, 2014;Stroud et al, 2014;Wolter et al, 2012).…”

Section: Introduction S0010mentioning

confidence: 99%

Functional and Genetic Analysis of Spectraplakins in Drosophila

Hahn¹,

Ronshaugen²,

Sánchez‐Soriano

et al. 2016

Methods in Enzymology

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“…1 Spectrin and other proteins such as actin, ankyrin, and protein 4.1 form a cytoskeletal network. 2,3 The most common and well studied spectrin isoforms are erythroid aIand bI-spectrin, and nonerythroid aII-and bII-spectrin. 1 It is generally accepted that aI-, aII-, bI-, and bII-spectrin are all expressed within neurons, [4][5][6][7][8] with aI-and bI-spectrin found in neuronal cell bodies, dendrites, and postsynaptic terminals of neurons, 9 whereas aII-and bII-spectrin are found in the axon and presynaptic termini.…”

Section: Introductionmentioning

confidence: 99%

Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs

et al. 2011

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We have screened a human immunoglobulin single-chain variable fragment (scFv) phage library against the C-terminal tetramerization regions of erythroid and nonerythroid beta spectrin (bI-C1 and bII-C1, respectively) to explore the structural uniqueness of erythroid and nonerythroid b-spectrin isoforms. We have identified interacting scFvs, with clones ''G5'' and ''A2'' binding only to bI-C1, and clone ''F11'' binding only to bII-C1. The K d values, estimated by competitive enzyme-linked immunosorbent assay, of these scFvs with their target spectrin proteins were 0.1-0.3 lM. A more quantitative K d value from isothermal titration calorimetry experiments with the recombinant G5 and bI-C1 was 0.15 lM. The a-spectrin fragments (model proteins), aI-N1 and aII-N1, competed with the bI-C1, or bII-C1, binding scFvs, with inhibitory concentration (IC 50 ) values of~50 lM for aI-N1, and 0.5 lM for aII-N1. Our predicted structures of bI-C1 and bII-C1 suggest that the Helix B 0 of the Cterminal partial domain of bI differs from that of bII. Consequently, an unstructured region downstream of Helix B 0 in bI may interact specifically with the unstructured, complementarity determining region H1 of G5 or A2 scFv. The corresponding region in bII was helical, and bII did not bind G5 scFv. Our results suggest that it is possible for cellular proteins to differentially associate with the C-termini of different b-spectrin isoforms to regulate a-and b-spectrin association to form functional spectrin tetramers, and may sort b-spectrin isoforms to their specific cellular localizations.Keywords: beta spectrin; erythroid and nonerythroid; scFv; structural difference; affinity difference Abbreviations: aI-N1, a recombinant protein of aI-spectrin segment with residues 1-156; aI-spectrin, erythroid a-spectrin; aII-N1, a GST fusion protein of aII-spectrin segment with residues 1-147; aII-spectrin, nonerythroid a-spectrin; bI-C1, a GST fusion protein of bI-spectrin segment with residues 1898-2083; bI-C1D, a GST fusion protein of bI-spectrin segment with residues 1898-2070, that is, the residues 2071-2083 in bI-C1 were deleted; bI-spectrin, erythroid b-spectrin; bII-C1, a GST fusion protein of bII-spectrin segment with residues 1906-2093; bII-spectrin, nonerythroid b-spectrin; CD, circular dichroism; CDRs, complementarity determining regions; ELISA, enzyme-linked immunosorbent assay; EPR, electron paramagnetic resonance; GST, glutathione S-transferase; HRP, horseradish peroxidase; ITC, isothermal titration calorimetry; PBS, phosphate buffered saline at pH 7.4; rG5, recombinant G5, a single-chain variable fragment found to bind bI-C1; scFv, single-chain variable fragment.Yuanli Song's current address is

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Spectrin, α-Actinin, and Dystrophin

Cited by 120 publications

References 219 publications

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Spectraplakin family proteins – cytoskeletal crosslinkers with versatile roles

Functional and Genetic Analysis of Spectraplakins in Drosophila

Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs

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