End-binding proteins and Ase1/PRC1 define local functionality of structurally distinct parts of the microtubule cytoskeleton

Duellberg, Christian; Fourniol, Franck J.; Maurer, Sebastian P.; Roostalu, Johanna; Surrey, Thomas

doi:10.1016/j.tcb.2012.10.003

Cited by 45 publications

(50 citation statements)

References 123 publications

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“…This preference is especially useful for the organization of bipolar networks and is the reason for their specific localization to the antiparallel overlaps of the midzone. Bundling proteins from the PRC1/ase1/MAP65 family also serve as a landmark in the midzone and are known to recruit many other MAPs to the overlaps (Duellberg et al, 2013).…”

Section: Self-organization Of Microtubule Networkmentioning

confidence: 99%

“…The protein holding these overlapping microtubules together is ase1. Additionally ase1 recruits many other proteins to the midzone (Duellberg et al, 2013). These proteins can be studied in vitro separately, but it is more relevant to test these proteins in bundles and in combination with ase1.…”

Section: Ase1 Bundling Assaysmentioning

confidence: 99%

“…Where these interpolar microtubules meet, they are bundled with their plus ends. Bundling proteins from the PRC1/ase1/MAP65 family mediate this antiparallel bundling (Loïodice et al, 2005;Duellberg et al, 2013). The bundles are not static structures: the microtubules are dynamic and motors induce sliding between microtubules (Sagolla et al, 2003;Fu et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…Bundling proteins of the PRC1/ase1/MAP65 family are abundant in the antiparallel overlaps of the midzone in vivo (Duellberg et al, 2013). Proteins of this family bundle microtubules preferentially in an antiparallel configuration (Gaillard et al, 2008;Kapitein et al, 2008;Subramanian et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…One way of localizing regulators properly is by binding to specific Microtubule Associated Proteins (MAPs) that recognize specific microtubule features. EB1 and ase1 localize to growing microtubule ends and antiparallel overlaps respectively, thereby creating landmarks for other microtubule regulators (Duellberg et al, 2013). Both EB1 and ase1 recruit a diverse set of proteins.…”

Section: Introductionmentioning

confidence: 99%

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Control mechanisms of microtubule overlap regions

Jongerius¹

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Section: Self-organization Of Microtubule Networkmentioning

confidence: 99%

Section: Ase1 Bundling Assaysmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Control mechanisms of microtubule overlap regions

Jongerius¹

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Tubulin and Microtubules

Amos

2015

Encyclopedia of Life Sciences

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Microtubules are found in almost all types of eukaryotic cell. Their principal constituents are the highly conserved proteins of the tubulin family, in the form of longitudinal protofilaments of tubulin heterodimers. The conserved lateral interactions produce a characteristic 2D lattice. Tubulin structure and conformational changes are now known to atomic resolution. Its GTP‐dependent dynamic self‐assembly and disassembly is modulated by a host of other proteins. This dynamic activity and a more passive role as tracks for interaction with motor proteins, kinesin and dynein, allow microtubules to perform vital roles in various forms of cell motility. They are an essential component of cell division, provide oriented tracks for the transport of cellular organelles and vesicles and are responsible for the relative positioning of cellular compartments. Thus, they are important targets in the control of cancer cells, as their essential activity is severely affected by a variety of drugs. Key Concepts Tubulin heterodimers, consisting of highly homologous α‐ and β‐tubulin monomers, self‐assemble into a unique lattice with polar longitudinal ‘protofilaments’ The assembled sheet has a slightly variable curvature, producing microtubules, with around 13 protofilaments but not strictly defined unless they are grown from a γ‐tubulin template or given a curvature appropriate to exactly 13 protofilaments by accessory proteins The structure of microtubules has been solved to near‐atomic level both with GTP homologues bound to β‐tubulin and with GDP bound; also a depolymerised protofilament structure in a longitudinally curved conformation is known Hydrolysis of bound GTP enables microtubules to assemble with ‘dynamic instability’, behaviour that depends on stochastic disassembly when the GTP ‘cap’ is lost from a growing end Microtubule behaviour is modified by many different accessory proteins that may act just at the tips or everywhere on the lattice wall To play different roles according to their positions in cells, the properties of microtubules may vary owing to different tubulin isotypes and be modified by a wide range of associated proteins Changes can also vary with time (‘ageing’) as a result of post‐translational modification of tubulin and of some accessory proteins Microtubules are employed in axonemes of cilia and flagella, where the motor protein dynein interacts with them to produce beating while other linking components help control the wave‐form Cytoplasmic microtubules provide tracks for vesicles and other cargoes driven by kinesins and cytoplasmic dynein Mitotic and meiotic spindles are assembled from microtubules, which interact with kinetochores and with multiple motor proteins Microtubules are susceptible to many small molecules that depolymerise or hyperstabilise them and thus serve as anti‐cancer drugs.

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Kif1c regulates osteoclastic bone resorption as a downstream molecule of p130Cas

Kobayakawa

Matsubara

Mizokami

et al. 2019

Cell Biochemistry & Function

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Podosome formation in osteoclasts is an important initial step in osteoclastic bone resorption. Mice lacking c-Src (c-Src −/− ) exhibited osteopetrosis due to a lack of podosome formation in osteoclasts. We previously identified p130Cas (Crk-associated substrate [Cas]) as one of c-Src downstream molecule and osteoclast-specific p130Cas-deficient (p130Cas ΔOCL−/− ) mice also exhibited a similar phenotype to c-Src −/− mice, indicating that the c-Src/p130Cas plays an important role for bone resorption by osteoclasts. In this study, we performed a cDNA microarray and compared the gene profiles of osteoclasts from c-Src −/− or p130Cas ΔOCL−/− mice with wild-type (WT) osteoclasts to identify downstream molecules of c-Src/p130Cas involved in bone resorption. Among several genes that were commonly downregulated in both c-Src −/− and p130Cas ΔOCL−/− osteoclasts, we identified kinesin family protein 1c (Kif1c), which regulates the cytoskeletal organization. Reduced Kif1c expression was observed in both c-Src −/− and p130Cas ΔOCL−/− osteoclasts compared with WT osteoclasts. Kif1c exhibited a broad tissue distribution, including osteoclasts. Knockdown of Kif1c expression using shRNAs in WT osteoclasts suppressed actin ring formation. Kif1c overexpression restored bone resorption subsequent to actin ring formation in p130Cas ΔOCL−/− osteoclasts but not c-Src −/− osteoclasts, suggesting that Kif1c regulates osteoclastic bone resorption in the downstream of p130Cas (191 words).Significance of the study: We previously showed that the c-Src/p130Cas (Cas) plays an important role for bone resorption by osteoclasts. In this study, we identified Abbreviations: Cas, Crk-associated substrate; CIZ, Cas-interacting zinc-finger protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; Kif, kinesin superfamily protein; M-CSF, macrophage colony-stimulating factor; MMP, matrix metalloproteinase; PBS, phosphate-buffered saline; RANKL, receptor activator of NF-κB ligand; TRAP, tartrate-resistant acid phosphatase; α-MEM, α-minimal essential medium.

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End-binding proteins and Ase1/PRC1 define local functionality of structurally distinct parts of the microtubule cytoskeleton

Cited by 45 publications

References 123 publications

Control mechanisms of microtubule overlap regions

Control mechanisms of microtubule overlap regions

Tubulin and Microtubules

Kif1c regulates osteoclastic bone resorption as a downstream molecule of p130Cas

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