Microtubule acetylation regulates dynamics of KIF1C-powered vesicles and contact of microtubule plus ends with podosomes

Bhuwania, Ridhirama; Castro-Castro, Antonio; Linder, Stefan

doi:10.1016/j.ejcb.2014.07.006

Cited by 44 publications

(38 citation statements)

References 67 publications

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“…However, KIF1C (similar to another kinesin-3 family member KIF1A; Cai et al, 2009) moves with growing MT plus ends and thus prefers dynamic MT tracks rather than stable ones. Moreover, MT acetylation, typical for stable MTs, suppresses movement of vesicles associated with KIF1C (Bhuwania et al, 2014). Accordingly, we suggest that dynamic CLASP-associated MTs normally serve as preferred tracks for KIF1C transport, and that relocation of CLASPs to peripheral MTs upon PDBu treatment facilitates KIF1C translocation to the lamella and, subsequently, triggers podosome formation (Fig.…”

Section: Discussionmentioning

confidence: 95%

Podosome-regulating kinesin KIF1C translocates to the cell periphery in a CLASP-dependent manner

Efimova

Grimaldi

Bachmann

et al. 2014

Journal of Cell Science

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The kinesin KIF1C is known to regulate podosomes, actin-rich adhesion structures, which remodel the extracellular matrix during physiological processes. Here we show that KIF1C is a player in the podosome-inducing signaling cascade. Upon induction of podosome formation by protein kinase C, KIF1C translocation to the cell periphery intensifies and KIF1C accumulates in the proximity of peripheral microtubules enriched with plus tip-associated proteins CLASPs and around podosomes. Importantly, without CLASPs, both KIF1C trafficking and podosome formation are suppressed. Moreover, chimeric mitochondria-targeted CLASP2 recruits KIF1C, suggesting a transient CLASP-KIF1C association. We propose that CLASP creates preferred microtubule tracks for KIF1C to promote podosome induction downstream of PKC.

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Section: Discussionmentioning

confidence: 95%

Podosome-regulating kinesin KIF1C translocates to the cell periphery in a CLASP-dependent manner

Efimova

Grimaldi

Bachmann

et al. 2014

Journal of Cell Science

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“…Like the finding in COS cells, the negative result could be due to the lack of modified microtubules in these cells rather than a different property of the motor, and this would require further investigation to elucidate. The sub cellular localization of KIF1C is regulated by acetylation in primary human macrophages in a way that suggests that tubulin acetylation is a negative signal for KIF1C transport [108]. Likewise, KIF1Bβ and KIF1A have been reported to drive lysosomal transport preferentially along tyrosinated (i.e.…”

Section: Specificity For a Subset Of Microtubule Tracksmentioning

confidence: 96%

“…This could be either due to the preference for unmodified (i.e. freshly assem bled) microtubules [108], or due to its fast transport speed and thus ability to catch up with the growing microtubule end [51], or due to its interaction with CLASP [119].…”

Section: Specificity For a Subset Of Microtubule Tracksmentioning

confidence: 99%

Intracellular cargo transport by kinesin-3 motors

Siddiqui

Straube

2017

Biochemistry Moscow

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Abstract-Intracellular transport along microtubules enables cellular cargoes to efficiently reach the extremities of large, eukaryotic cells. While it would take more than 200 years for a small vesicle to diffuse from the cell body to the growing tip of a one meter long axon, transport by a kinesin allows delivery in one week. It is clear from this example that the evolution of intracellular transport was tightly linked to the development of complex and macroscopic life forms. The human genome encodes 45 kinesins, 8 of those belonging to the family of kinesin 3 organelle transporters that are known to transport a vari ety of cargoes towards the plus end of microtubules. However, their mode of action, their tertiary structure, and regulation are controversial. In this review, we summarize the latest developments in our understanding of these fascinating molecular motors.

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“…Loss of microtubule acetylation was reported to reduce the binding and motility of the molecular motor kinesin-1 in vitro [118]. Related to this, kinesin-1 and a kinesin-like protein preferably bind to stable microtubules marked by acetylation and detyrosination [119,120]. Increased tubulin acetylation by HDAC6 inhibition causes recruitment of dynein and kinesin-1 to microtubules, thereby compensating intracellular transport deficits in Huntington's disease [121].…”

Section: Tubulin Acetylation and Intracellular Transportmentioning

confidence: 99%

Tubulin acetylation: responsible enzymes, biological functions and human diseases

Yang

2015

Cell. Mol. Life Sci.

213

184

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Microtubules have important functions ranging from maintenance of cell morphology to subcellular transport, cellular signaling, cell migration, and formation of cell polarity. At the organismal level, microtubules are crucial for various biological processes, such as viral entry, inflammation, immunity, learning and memory in mammals. Microtubules are subject to various covalent modifications. One such modification is tubulin acetylation, which is associated with stable microtubules and conserved from protists to humans. In the past three decades, this reversible modification has been studied extensively. In mammals, its level is mainly governed by opposing actions of α-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6). Knockout studies of the mouse enzymes have yielded new insights into biological functions of tubulin acetylation. Abnormal levels of this modification are linked to neurological disorders, cancer, heart diseases and other pathological conditions, thereby yielding important therapeutic implications. This review summarizes related studies and concludes that tubulin acetylation is important for regulating microtubule architecture and maintaining microtubule integrity. Together with detyrosination, glutamylation and other modifications, tubulin acetylation may form a unique 'language' to regulate microtubule structure and function.

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Microtubule acetylation regulates dynamics of KIF1C-powered vesicles and contact of microtubule plus ends with podosomes

Cited by 44 publications

References 67 publications

Podosome-regulating kinesin KIF1C translocates to the cell periphery in a CLASP-dependent manner

Podosome-regulating kinesin KIF1C translocates to the cell periphery in a CLASP-dependent manner

Intracellular cargo transport by kinesin-3 motors

Tubulin acetylation: responsible enzymes, biological functions and human diseases

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