DDA3 and Mdp3 modulate Kif2a recruitment onto the mitotic spindle to control minus-end spindle dynamics

Kwon, Hye Jin; Park, Ji Eun; Song, Haiyu; Jang, Chang-Young

doi:10.1242/jcs.180109

Cited by 19 publications

(10 citation statements)

References 23 publications

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“…KIF2A, which is a type of motor protein with an oncogenic function, has been identified to be overexpressed in a number of human cancers (15,23). KIF2A is a member of the kinesin-13 family of proteins, and serves the function of depolymerizing the ends of microtubules (MTs) (24,25). MTs are vital components of the cytoskeleton and are involved in the invasion and metastasis of cancer (26,27).…”

Section: Discussionmentioning

confidence: 99%

Effects of KIF2A on the prognosis of nasopharyngeal carcinoma and nasopharyngeal carcinoma cells

Zhang

Liu

et al. 2019

Oncol Lett

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Nasopharyngeal carcinoma (NPC) is a common tumor in south China. Kinesin family member 2A (KIF2A) belongs to the kinesin-13 family and is associated with the growth and invasion of a number of different types of human cancer, including ovarian, breast and prostate cancer. The aim of the present study was to evaluate the expression of KIF2A in NPC and explore the relationship between KIF2A and the basic characteristics of 5-8F cells. Immunohistochemistry was performed on tissues from 97 patients with NPC to assess KIF2A protein expression. KIF2A was knocked down by a specific short interfering (si)RNA in 5-8F cell lines. Cell proliferation, apoptosis and cycle were analyzed by MTT assay and flow cytometry. The invasive ability and angiogenesis were evaluated by Matrigel assay and reverse transcription-quantitative PCR. The level of KIF2A was associated with the growth and migration of primary tumor, nodal status and tumor stage. The viability of KIF2A-knockdown cells was decreased compared with that of the control cells. The number of apoptotic cells, as well as the percentage of cells in the G0/G1 phase, was higher in the KIF2A siRNA group compared with the control group. The invasive and angiogenetic ability of 5-8F cells in the KIF2A siRNA group was decreased compared with the control group. In conclusion, the expression of KIF2A correlated with the poor clinicopathological features in NPC. Therefore, KIF2A may serve an important role in the progression of NPC and proliferation of 5-8F cells, which might present a potential therapeutic target for patients with NPC.

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Section: Discussionmentioning

confidence: 99%

Effects of KIF2A on the prognosis of nasopharyngeal carcinoma and nasopharyngeal carcinoma cells

Zhang

Liu

et al. 2019

Oncol Lett

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“…It is unlikely that this was due to the lack of kinesin-1-mediated transport, as KIF5B knockout cells displayed no apparent growth or proliferation defects, and the two other kinesin-1 isoforms, KIF5A and KIF5C, do not seem to be expressed in HeLa cells (Nagaraj et al, 2011). Although MAP7 was shown to be phosphorylated and thus inactivated during mitosis (McHedlishvili et al, 2018), it is possible that MAP7 proteins still contribute to cell division, as ensconsin is known to participate in spindle formation in flies (Gallaud et al, 2014), and MAP7D3 was reported to modulate the recruitment of kinesin-13 to the mitotic spindle (Kwon et al, 2016). In order to remove all three MAP7 homologues simultaneously, we performed siRNA-mediated knockdown of MAP7D1 and MAP7D3 in the stable MAP7 knockout line, and this approach resulted in an efficient loss of all three MAP7 family members (Fig.…”

Section: Map7 Family Members Act Redundantly In Mitochondrial Distribmentioning

confidence: 99%

MAP7 family proteins regulate kinesin-1 recruitment and activation

Hooikaas

Martin

Mühlethaler

et al. 2018

Preprint

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Kinesin-1 is responsible for microtubule-based transport of numerous cellular cargoes. Here, we explored the regulation of kinesin-1 by MAP7/ensconsin family proteins. We found that all four mammalian MAP7 family members bound to kinesin-1, and MAP7, MAP7D1 and MAP7D3 acted redundantly to enable kinesin-1-dependent transport in HeLa cells. Microtubule recruitment of the truncated kinesin-1 KIF5B-560, which contains the stalk but not the cargo-binding and autoregulatory regions, was inhibited in cells co-depleted of these three MAP7 proteins. In vitro, purified MAP7 and MAP7D3 increased microtubule landing rate and processivity of KIF5B-560.The same was true for MAP7D3 C-terminus, which weakly bound to microtubules and exchanged rapidly on motile KIF5B-560 motors. A C-terminal MAP7 fragment lacking microtubule affinity increased KIF5B-560 recruitment to microtubules in vitro and in cells, and partially rescued kinesin-1-dependent transport in the absence of full-length MAP7 proteins. We propose that MAP7 proteins are microtubule-tethered kinesin-1 activators, with which the motor transiently interacts as it moves along microtubules. SummaryA combination of experiments in cells and in vitro reconstitution assays demonstrated that mammalian MAP7 family proteins act redundantly to activate kinesin-1 and promote its microtubule binding and processivity by transiently associating with the stalk region of the motor.All rights reserved. No reuse allowed without permission.was not peer-reviewed) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.

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“…CEP170 is a MT-binding protein present at centriolar sub-distal appendages/basal feet, that is required for the recruitment of MT and actin-associated ciliogenesis regulators to the mother centriole/basal body (Copeland et al, 2018). Another centrosome-related prey, identified only in cycling cells was MAP7D3, a MT-binding protein that regulates MT assembly and stability, being important for MT dynamics at spindle poles (Kwon et al, 2016;Sun et al, 2011;Yadav et al, 2014). Under serum starvation, we identified MRE11A and PPP1CA.…”

Section: Resultsmentioning

confidence: 92%

LUZP1 and the tumour suppressor EPLIN are negative regulators of primary cilia formation

Gonçalves

Coyaud

Laurent

et al. 2019

Preprint

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Running title: LUZP1 and EPLIN regulate ciliogenesis SUMMARY Gonçalves et al. show that LUZP1 and its interactor EPLIN are negative regulators of ciliogenesis. LUZP1 is a novel actin-stabilizing protein localizing at the centrosome and basal body where it may regulate actin-associated processes. 2 ABSTRACT Cilia/flagella are microtubule-based cellular projections with important sensory and motility functions. Their absence or malfunction is associated with a growing number of human diseases collectively referred to as ciliopathies. However, the fundamental mechanisms underpinning cilia biogenesis and functions remain only partly understood. Here, we show that LUZP1, and its interacting protein EPLIN, are negative regulators of primary cilia formation. LUZP1 is an actinassociated protein that localizes to both actin filaments and the centrosome/basal body. Like EPLIN, LUZP1 is an actin-stabilizing protein and likely regulates actin dynamics at the centrosome. Both proteins interact with ciliogenesis and cilia length regulators, and are potential players in the actin-dependent processes involved in centrosome to basal body conversion. Ciliogenesis deregulation caused by LUZP1 or EPLIN loss may contribute to the pathology of their associated diseases.

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DDA3 and Mdp3 modulate Kif2a recruitment onto the mitotic spindle to control minus-end spindle dynamics

Cited by 19 publications

References 23 publications

Effects of KIF2A on the prognosis of nasopharyngeal carcinoma and nasopharyngeal carcinoma cells

Effects of KIF2A on the prognosis of nasopharyngeal carcinoma and nasopharyngeal carcinoma cells

MAP7 family proteins regulate kinesin-1 recruitment and activation

LUZP1 and the tumour suppressor EPLIN are negative regulators of primary cilia formation

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