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

Efimova, Nadia; Grimaldi, Ashley D; Bachmann, Alice; Frye, Keyada; Zhu, Xiaodong; Feoktistov, Alexander; Straube, Anne; Kaverina, Irina

doi:10.1242/jcs.149633

Cited by 36 publications

(71 citation statements)

References 59 publications

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“…Multiple microtubule-associated factors, including kinesins KIF1C, KIF5B, KIF3A/B and KIF9, +TIPs EB1 and CLASP1, as well as deacetylase HDAC6, have been linked to the formation of podosomes (Bhuwania et al, 2014;Biosse et al, 2014;Cornfine et al, 2011;Destaing et al, 2005;Efimova et al, 2014;Maridonneau-Parini, 2014;Wiesner et al, 2010;Zhu et al, 2016). Podosomes, which are characterized by specialized organization of actin and adhesion molecules and the ability to degrade ECM, thus appear to depend on different aspects of microtubule regulation and microtubule-based transport for their function.…”

Section: Microtubule-associated Proteins In 3d Cell Migrationspecificmentioning

confidence: 99%

Microtubules in 3D cell motility

Bouchet

Akhmanova

2017

Journal of Cell Science

104

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Three-dimensional (3D) cell motility underlies essential processes, such as embryonic development, tissue repair and immune surveillance, and is involved in cancer progression. Although the cytoskeleton is a well-studied regulator of cell migration, most of what we know about its functions originates from studies conducted in twodimensional (2D) cultures. This research established that the microtubule network mediates polarized trafficking and signaling that are crucial for cell shape and movement in 2D. In parallel, developments in light microscopy and 3D cell culture systems progressively allowed to investigate cytoskeletal functions in more physiologically relevant settings. Interestingly, several studies have demonstrated that microtubule involvement in cell morphogenesis and motility can differ in 2D and 3D environments. In this Commentary, we discuss these differences and their relevance for the understanding the role of microtubules in cell migration in vivo. We also provide an overview of microtubule functions that were shown to control cell shape and motility in 3D matrices and discuss how they can be investigated further by using physiologically relevant models.

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Section: Microtubule-associated Proteins In 3d Cell Migrationspecificmentioning

confidence: 99%

Microtubules in 3D cell motility

Bouchet

Akhmanova

2017

Journal of Cell Science

104

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“…It is thought that kinesin 3 motors cooperate with dynein for bidirectional motility, so whether PTL 1 affects Unc 104 directly or negatively regulates dynein to cause the observed phenotype remains to be elucidated. The microtubule plus end tracking protein CLASP is required to stimulate the trafficking of KIF1C [119]. KIF1C has also been described to move with growing microtubule plus ends in cells [120].…”

Section: Specificity For a Subset Of Microtubule Tracksmentioning

confidence: 99%

“…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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“…The CLASPs (CLASP1 and CLASP2), discovered in 2001 as binding partners for the CAP-Gly domain-containing linker proteins 1 and 2 (CLIP1/CLIP-170 and CLIP2/CLIP-115), were initially found to bind and stabilize the growing, distal ends of microtubules, independently of the CLIPs (17). Subsequent studies revealed that CLASPs localize wherever microtubules are needed, kinetochores in the nucleus for mitosis (18)(19)(20)(21)(22)(23), the cell cortex (24-27), the leading edge lamella and lamellipodium of motile cells (28)(29)(30)(31), the Golgi (17,(32)(33)(34)(35)(36)(37)(38), axons (39, 40), the developing apical membrane surface during lumen formation within endothelial cells (41), adherens junctions at cell-cell contacts (42, 43), the neuromuscular junction (44)(45)(46), podosomes (47), and focal adhesions (48). Within each of these molecular systems, the dynamic instability of microtubules undergo differential regulation by proteins specific to each of the biological processes (49)(50)(51)(52)(53)(54)(55).…”

Section: Introductionmentioning

confidence: 99%

Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein

Kruse

Krantz

Barker

et al. 2017

Molecular & Cellular Proteomics

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SummaryCLASP2 is a microtubule-associated protein that undergoes insulin-stimulated phosphorylation and co-localization with reorganized actin and GLUT4 at the plasma membrane.To gain insight to the role of CLASP2 in this system, we developed and successfully executed a streamlined interactome approach and built a CLASP2 protein network in 3T3-L1 adipocytes.Using two different commercially available antibodies for CLASP2 and an antibody for epitopetagged, overexpressed CLASP2, we performed multiple affinity purification coupled with mass spectrometry (AP-MS) experiments in combination with label-free quantitative proteomics and analyzed the data with the bioinformatics tool Significance Analysis of Interactome (SAINT). We discovered that CLASP2 co-immunoprecipitates (co-IPs) the novel protein SOGA1, the microtubule-associated protein kinase MARK2, and the microtubule/actin-regulating protein G2L1. The GTPase-activating proteins AGAP1 and AGAP3 were also enriched in the CLASP2 interactome, although subsequent AGAP3 and CLIP2 interactome analysis suggests a preference of AGAP3 for CLIP2. Follow-up MARK2 interactome analysis confirmed reciprocal co-IP of CLASP2 and also revealed MARK2 can co-IP SOGA1, glycogen synthase, and glycogenin.Investigating the SOGA1 interactome confirmed SOGA1 can reciprocal co-IP both CLASP2 and MARK2 as well as glycogen synthase and glycogenin. SOGA1 was confirmed to colocalize with CLASP2 and also with tubulin, which identifies SOGA1 as a new microtubule-associated protein.These results introduce the metabolic function of these proposed novel protein networks and their relationship with microtubules as new fields of cytoskeleton-associated protein biology. 5

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

Cited by 36 publications

References 59 publications

Microtubules in 3D cell motility

Microtubules in 3D cell motility

Intracellular cargo transport by kinesin-3 motors

Characterization of the CLASP2 Protein Interaction Network Identifies SOGA1 as a Microtubule-Associated Protein

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