LMO7 exerts an effect on mitosis progression and the spindle assembly checkpoint

Tzeng, Yao-Wei; Li, Dai-Yu; Chen, Yvan; Yang, Cheng-Hsiu; Chang, Chih-Yun; Juang, Yue‐Li

doi:10.1016/j.biocel.2017.11.006

Cited by 9 publications

(10 citation statements)

References 42 publications

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“…LIM domains contain tandem zinc-finger structures and function as a modular protein-binding interfaces (reviewed in te Velthuis et al (2007)). Both proteins were shown to associate with actin structures and play a role in cancer progression (Tzeng et al 2018; Zhang et al . 2007).…”

Section: Resultsmentioning

confidence: 99%

“…LMO7 is reported to bind the nuclear membrane protein EMERIN which is a key player in Emery–Dreifuss muscular dystrophy. Moreover, it shuttles between the plasma membrane and the nucleus (Holaska, Rais-Bahrami, and Wilson 2006) and seems to control mitosis progression and exerts an effect on the spindle assembly checkpoint (Tzeng et al 2018). LMO7 is also localized at focal adhesions (Wozniak et al 2013).…”

Section: Resultsmentioning

confidence: 99%

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An Interaction Network of the Human SEPT9 Established by Quantitative Mass Spectrometry

Hecht

Rösler

Wiese

et al. 2019

G3 Genes|Genomes|Genetics

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Septins regulate the organization of the actin cytoskeleton, vesicle transport and fusion, chromosome alignment and segregation, and cytokinesis in mammalian cells. SEPT9 is part of the core septin hetero-octamer in human cells which is composed of SEPT2, SEPT6, SEPT7, and SEPT9. SEPT9 has been linked to a variety of intracellular functions as well as to diseases and diverse types of cancer. A targeted high-throughput approach to systematically identify the interaction partners of SEPT9 has not yet been performed. We applied a quantitative proteomics approach to establish an interactome of SEPT9 in human fibroblast cells. Among the newly identified interaction partners were members of the myosin family and LIM domain containing proteins. Fluorescence microscopy of SEPT9 and its interaction partners provides additional evidence that SEPT9 might participate in vesicle transport from and to the plasma membrane as well as in the attachment of actin stress fibers to cellular adhesions.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

An Interaction Network of the Human SEPT9 Established by Quantitative Mass Spectrometry

Hecht

Rösler

Wiese

et al. 2019

G3 Genes|Genomes|Genetics

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“…On the other hand, it is known, that Flaviviruses enter host cells through the process of clathrin-mediated endocytosis [127, 128]. Thus, MSR1 may interfere with this process.2. LMO7 51 LMO7 gene encodes LIM domain only protein 7 with three conserved domains: (1) the CH (Calponin Homology) domain, known to confer the actin -binding ability on many actin -associated proteins; (2) the PDZ domain, a region containing a conserved Gly-Leu-Gly-Phe repeat sequence, may take part in protein targeting and protein complex assembly; (3) LIM (Lin-11-Isl-1-Mec-3) domain, that may regulate transcription or cytoskeleton assembly [129]. Thus LMO7 is known to be a nucleocytoplasmic shuttling protein that possesses both actin -binding and transcription regulator activities [130].…”

Section: Discussionmentioning

confidence: 99%

Exome-wide search and functional annotation of genes associated in patients with severe tick-borne encephalitis in a Russian population

et al. 2019

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Background Tick-borne encephalitis (TBE) is a viral infectious disease caused by tick-borne encephalitis virus (TBEV). TBEV infection is responsible for a variety of clinical manifestations ranging from mild fever to severe neurological illness. Genetic factors involved in the host response to TBEV that may potentially play a role in the severity of the disease are still poorly understood. In this study, using whole-exome sequencing, we aimed to identify genetic variants and genes associated with severe forms of TBE as well as biological pathways through which the identified variants may influence the severity of the disease. Results Whole-exome sequencing data analysis was performed on 22 Russian patients with severe forms of TBE and 17 Russian individuals from the control group. We identified 2407 candidate genes harboring rare, potentially pathogenic variants in exomes of patients with TBE and not containing any rare, potentially pathogenic variants in exomes of individuals from the control group. According to DAVID tool, this set of 2407 genes was enriched with genes involved in extracellular matrix proteoglycans pathway and genes encoding proteins located at the cell periphery. A total of 154 genes/proteins from these functional groups have been shown to be involved in protein-protein interactions (PPIs) with the known candidate genes/proteins extracted from TBEVHostDB database. By ranking these genes according to the number of rare harmful minor alleles, we identified two genes ( MSR1 and LMO7), harboring five minor alleles, and three genes ( FLNA, PALLD, PKD1 ) harboring four minor alleles. When considering genes harboring genetic variants associated with severe forms of TBE at the suggestive P -value < 0.01, 46 genes containing harmful variants were identified. Out of these 46 genes, eight ( MAP4, WDFY4, ACTRT2, KLHL25, MAP2K3, MBD1, OR10J1, and OR2T34) were additionally found among genes containing rare pathogenic variants identified in patients with TBE; and five genes ( WDFY4 , ALK, MAP4, BNIPL, EPPK1 ) were found to encode proteins that are involved in PPIs with proteins encoded by genes from TBEVHostDB. Three genes out of five ( MAP4, EPPK1, ALK ) were found to encode proteins located at cell periphery. Conclusions Whole-exome sequencing followed by systems biology approach enabled to identify eight candidate genes ( MAP4, WDFY4, ACTRT2, KLHL25, MAP2K3, MBD1, OR10J1, and OR2T34 ) that can potentially determine predisposition to severe forms of TBE. Analyses of the genetic risk factors for severe forms of TBE revealed a significant enrichment with genes controlling extracellular matrix proteoglycans pathway as well...

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“…LIM domains contain tandem zinc-finger structures and function as a modular protein-binding interfaces (reviewed in [31]). Both proteins were shown to associate with actin structures and play a role in cancer progression [32,33]. One more LIM domain containing protein, LIMA1 (herein from now on referred to as EPLIN, the product of the LIMA1 gene), was identified with a LOG 2 (H/L)>2 in one of the replicates, however below the SigB threshold.…”

Section: Resultsmentioning

confidence: 99%

“…A contribution of SEPT9 in vesicle transport and docking can be anticipated since other constituents of the vesicle trafficking machinery (VAMP2, VABP, COPA, SEC22B) were already identified in a high throughput MS screen as presumable SEPT9 interactors [41]. shuttles between the plasma membrane and the nucleus [42] and seems to control mitosis progression and exerts an effect on the splindle assembly chekpoint [32].…”

Section: Resultsmentioning

confidence: 99%

An interaction network of the human SEPT9 established by quantitative mass spectrometry reveals an interplay with myosin motors

Hecht

Rösler

Wiese

et al. 2018

Preprint

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Phenotypic variations of an organism or a single cell often arise from alterations of protein interaction networks. We provide here an interaction network of the human SEPT9, an important component of the human septin cytoskeleton. AbstractExperimentally deciphering and understanding the interaction network of a particular protein provides often evidence for so far unknown functions. For the septins, a class of cytoskeletal proteins, targeted high-throughput approaches that aim at systematically deciphering interaction partners have not yet been performed. Septins regulate the organization of the acin cytoskeleton, vesicle transport and fusion, chromosome alignment-and segregation, and cytokinesis. SEPT9 is part of the core septin hetero-octamer in human cells which is composed of SEPT2, SEPT6, SEPT7, and SEPT9. SEPT9 has been linked to a variety of intracellular functions as well as to diseases and diverse types of cancer. We applied a quantitative proteomics approach to establish an interactome of SEPT9 in human fibroblast cells. We identified among others so far unknown interaction partners from the myosin family and could provide evidence that SEPT9 participates in vesicle transport from and to the plasma membrane as well as in the attachment of actin stress fibers to cellular adhesions.

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LMO7 exerts an effect on mitosis progression and the spindle assembly checkpoint

Cited by 9 publications

References 42 publications

An Interaction Network of the Human SEPT9 Established by Quantitative Mass Spectrometry

An Interaction Network of the Human SEPT9 Established by Quantitative Mass Spectrometry

Exome-wide search and functional annotation of genes associated in patients with severe tick-borne encephalitis in a Russian population

An interaction network of the human SEPT9 established by quantitative mass spectrometry reveals an interplay with myosin motors

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