CAP-Gly proteins contribute to microtubule-dependent trafficking via interactions with the C-terminal aromatic residue of α-tubulin

Andrieux, Annie; Aubry, Laurence; Boscheron, Cécile

doi:10.1080/21541248.2016.1277002

Cited by 8 publications

(7 citation statements)

References 54 publications

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“…ACF7; also known as MACF1) and motors mediate the static and dynamic structural associations, respectively (Rodriguez et al, 2003). On the other hand, the dynamics of actin and microtubules feed back to upstream signaling cascades, including small GTPases such as RhoA and Rac1, to indirectly affect each other (Palazzo et al, 2001;Wittmann and Waterman-Storer, 2001; Krendel et al, 2002;Boscheron et al, 2016;Andrieux et al, 2017). Recently, the connection between actin and microtubule post-translational modifications (PTMs) has been suggested as another form of intercytoskeletal crosstalk (Fernandez-Barrera et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Arp2/3-branched actin regulates microtubule acetylation levels and affects mitochondrial distribution

Shi

Yuan

Huang

et al. 2019

Journal of Cell Science

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Actin and microtubule cytoskeletons regulate cell morphology, participate in organelle trafficking and function in response to diverse environmental cues. Precise spatial-temporal coordination between these two cytoskeletons is essential for cells to live and move. Here, we report a novel crosstalk between actin and microtubules, in which the branched actin maintains microtubule organization, dynamics and stability by affecting tubulin acetylation levels. We observed that acetylated tubulin significantly decreases upon perturbation of the Arp2/3-branched actin. We subsequently discover that HDAC6 participates in this process by altering its interaction with tubulin and the Arp2/3-stabilizer cortactin. We further identify that the homeostasis of branched actin controls mitochondrial distribution via this microtubule acetylation-dependent mechanism. Our findings shed new light on the integral view of cytoskeletal networks, highlighting post-translational modification as another possible form of cytoskeletal inter-regulation, aside from the established crosstalks through structural connection or upstream signaling pathways.

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Section: Introductionmentioning

confidence: 99%

Arp2/3-branched actin regulates microtubule acetylation levels and affects mitochondrial distribution

Shi

Yuan

Huang

et al. 2019

Journal of Cell Science

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“…These +TIPs contribute to loading cargo onto MTs for minus‐end‐directed transport towards the cell center . CLIP‐170 has a key role in linking MTs to membrane trafficking . CLIP‐170 has been suggested to be critical for the migration of EGFR‐containing endosomes through a dynein‐driven transport .…”

Section: Introductionmentioning

confidence: 99%

“…32,33 CLIP-170 has a key role in linking MTs to membrane trafficking. 34 CLIP-170 has been suggested to be critical for the migration of EGFR-containing endosomes through a dynein-driven transport. 35 However, to date, our understanding of how the MT-based machinery functions in endocytic trafficking of RTKs remains poorly understood.…”

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confidence: 99%

CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration

Zaoui

Duhamel

Parachoniak

et al. 2019

Traffic

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Endocytic sorting of activated receptor tyrosine kinases (RTKs), alternating between recycling and degradative processes, controls signal duration, location and surface complement of RTKs. The microtubule (MT) plus‐end tracking proteins (+TIPs) play essential roles in various cellular activities including translocation of intracellular cargo. However, mechanisms through which RTKs recycle back to the plasma membrane following internalization in response to ligand remain poorly understood. We report that net outward‐directed movement of endocytic vesicles containing the hepatocyte growth factor (HGF) Met RTK, requires recruitment of the +TIP, CLIP‐170, as well as the association of CLIP‐170 to MT plus‐ends. In response to HGF, entry of Met into Rab4‐positive endosomes results in Golgi‐localized γ‐ear‐containing Arf‐binding protein 3 (GGA3) and CLIP‐170 recruitment to an activated Met RTK complex. We conclude that CLIP‐170 co‐ordinates the recycling and the transport of Met‐positive endocytic vesicles to plus‐ends of MTs towards the cell cortex, including the plasma membrane and the lamellipodia, thereby promoting cell migration.

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“…These modifications occur in α-tubulin isotypes and consist of the addition and removal of a C-terminal tyrosine residue. With the exception of TUBA4A and TUBA8, that present a C-terminal phenylalanine, all α-tubulin isotypes expose a C-terminal tyrosine residue, which can be removed by detyrosination and re-added by tyrosination [ 134 ]. Thus, detyrosination is the initial step that triggers the detyrosination–tyrosination cycle.…”

Section: Neuronal Microtubules: Regulative Mechanismsmentioning

confidence: 99%

Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases

Sferra

Nicita

Bertini

2020

IJMS

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Neurons are particularly susceptible to microtubule (MT) defects and deregulation of the MT cytoskeleton is considered to be a common insult during the pathogenesis of neurodegenerative disorders. Evidence that dysfunctions in the MT system have a direct role in neurodegeneration comes from findings that several forms of neurodegenerative diseases are associated with changes in genes encoding tubulins, the structural units of MTs, MT-associated proteins (MAPs), or additional factors such as MT modifying enzymes which modulating tubulin post-translational modifications (PTMs) regulate MT functions and dynamics. Efforts to use MT-targeting therapeutic agents for the treatment of neurodegenerative diseases are underway. Many of these agents have provided several benefits when tested on both in vitro and in vivo neurodegenerative model systems. Currently, the most frequently addressed therapeutic interventions include drugs that modulate MT stability or that target tubulin PTMs, such as tubulin acetylation. The purpose of this review is to provide an update on the relevance of MT dysfunctions to the process of neurodegeneration and briefly discuss advances in the use of MT-targeting drugs for the treatment of neurodegenerative disorders.

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CAP-Gly proteins contribute to microtubule-dependent trafficking via interactions with the C-terminal aromatic residue of α-tubulin

Cited by 8 publications

References 54 publications

Arp2/3-branched actin regulates microtubule acetylation levels and affects mitochondrial distribution

Arp2/3-branched actin regulates microtubule acetylation levels and affects mitochondrial distribution

CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration

Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases

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