KIFC3 promotes mitotic progression and integrity of the central spindle in cytokinesis

Nachbar, Jeannette; Lázaro‐Diéguez, Francisco; Prekeris, Rytis; Cohen, David; Müsch, Anne

doi:10.4161/cc.27266

Cited by 6 publications

(2 citation statements)

References 29 publications

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“…Finally, none of the predictors was able to detect the succinylation sites of other proteins. A few examples are lon protease homolog (UniProtKB ID Q8CGK3) which recognises and degrades unfolded proteins [ 81 ], caveolin (UniProtKB ID D3Z0J2) which is involved in vesicular transport, cholesterol homeostasis, signal transduction and tumor suppression [ 82 ], and kinesin-like protein (UniProtKB ID E9PWU7) that caps microtubules released from the centrosome during interphase [ 83 ].…”

Section: Resultsmentioning

confidence: 99%

Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction

et al. 2018

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BackgroundPost-translational modification is considered an important biological mechanism with critical impact on the diversification of the proteome. Although a long list of such modifications has been studied, succinylation of lysine residues has recently attracted the interest of the scientific community. The experimental detection of succinylation sites is an expensive process, which consumes a lot of time and resources. Therefore, computational predictors of this covalent modification have emerged as a last resort to tackling lysine succinylation.ResultsIn this paper, we propose a novel computational predictor called ‘Success’, which efficiently uses the structural and evolutionary information of amino acids for predicting succinylation sites. To do this, each lysine was described as a vector that combined the above information of surrounding amino acids. We then designed a support vector machine with a radial basis function kernel for discriminating between succinylated and non-succinylated residues. We finally compared the Success predictor with three state-of-the-art predictors in the literature. As a result, our proposed predictor showed a significant improvement over the compared predictors in statistical metrics, such as sensitivity (0.866), accuracy (0.838) and Matthews correlation coefficient (0.677) on a benchmark dataset.ConclusionsThe proposed predictor effectively uses the structural and evolutionary information of the amino acids surrounding a lysine. The bigram feature extraction approach, while retaining the same number of features, facilitates a better description of lysines. A support vector machine with a radial basis function kernel was used to discriminate between modified and unmodified lysines. The aforementioned aspects make the Success predictor outperform three state-of-the-art predictors in succinylation detection.Electronic supplementary materialThe online version of this article (10.1186/s12864-017-4336-8) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction

et al. 2018

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“…KIFC3 is ubiquitously present throughout the human body (65) and is abundantly expressed in the human retinal pigment epithelium and in the outer plexiform layer of the retina (66). KIFC3 is also important for GA positioning and structure maintenance (67) and recent research has indicated that KIFC3 might cap and deliver free MTs to their final destination (68). Remarkably, however, KIFC3 knockout mice are viable and develop normally (65), suggesting that other proteins may have overlapping roles or that other proteins can compensate for the role of KIFC3.…”

Section: Discussionmentioning

confidence: 99%

Interactome analysis reveals that FAM161A, deficient in recessive retinitis pigmentosa, is a component of the Golgi-centrosomal network

Gioia

Farinelli

Letteboer

et al. 2015

Human Molecular Genetics

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Defects in FAM161A, a protein of unknown function localized at the cilium of retinal photoreceptor cells, cause retinitis pigmentosa, a form of hereditary blindness. By using different fragments of this protein as baits to screen cDNA libraries of human and bovine retinas, we defined a yeast two-hybrid-based FAM161A interactome, identifying 53 bona fide partners. In addition to statistically significant enrichment in ciliary proteins, as expected, this interactome revealed a substantial bias towards proteins from the Golgi apparatus, the centrosome and the microtubule network. Validation of interaction with key partners by co-immunoprecipitation and proximity ligation assay confirmed that FAM161A is a member of the recently recognized Golgi-centrosomal interactome, a network of proteins interconnecting Golgi maintenance, intracellular transport and centrosome organization. Notable FAM161A interactors included AKAP9, FIP3, GOLGA3, KIFC3, KLC2, PDE4DIP, NIN and TRIP11. Furthermore, analysis of FAM161A localization during the cell cycle revealed that this protein followed the centrosome during all stages of mitosis, likely reflecting a specific compartmentalization related to its role at the ciliary basal body during the G0 phase. Altogether, these findings suggest that FAM161A's activities are probably not limited to ciliary tasks but also extend to more general cellular functions, highlighting possible novel mechanisms for the molecular pathology of retinal disease.

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A novel role of KIF3b in the seminoma cell cycle

Shen

Xiao

She

et al. 2017

Experimental Cell Research

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KIFC3 promotes mitotic progression and integrity of the central spindle in cytokinesis

Cited by 6 publications

References 29 publications

Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction

Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction

Interactome analysis reveals that FAM161A, deficient in recessive retinitis pigmentosa, is a component of the Golgi-centrosomal network

A novel role of KIF3b in the seminoma cell cycle

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