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anti-Human GPSM2 Anticorps:
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Human Polyclonal GPSM2 Primary Antibody pour ICC, IF - ABIN4315933
Kotak, Busso, Gönczy: NuMA interacts with phosphoinositides and links the mitotic spindle with the plasma membrane. dans The EMBO journal 2014
Show all 2 Pubmed References
Dog (Canine) Polyclonal GPSM2 Primary Antibody pour ELISA, WB - ABIN547839
Yasumi, Sakisaka, Hoshino, Kimura, Sakamoto, Yamanaka, Ohno, Takai: Direct binding of Lgl2 to LGN during mitosis and its requirement for normal cell division. dans The Journal of biological chemistry 2005
Study reports the crystal structure of NuMA:LGN hetero-hexamers, and unveil their role in promoting the assembly of active cortical dynein/dynactin motors that are required in orchestrating oriented divisions in polarized cells.
The results show how E-cadherin instructs the assembly of the LGN/NuMA complex at cell-cell contacts, and define a mechanism that couples cell division orientation to intercellular adhesion.
Endothelial flow mechanotransduction through the junctional complex is mediated by a specific pool of VE-cadherin that is phosphorylated on cytoplasmic tyrosine Y658 and bound to LGN.
In mammary stem cells, the asymmetric domain of Insc bound to LGN:Galphai(GDP) suffices to drive asymmetric fate, and reverts aberrant symmetric divisions induced by p53 loss.
Data support the notion that the Galpha, but not Gbetagamma, arm of the Gi/o signalling is involved in TRPC4 activation and unveil new roles for RGS and LGN in fine-tuning TRPC4 activities.
high expression of G-protein signaling modulator 2 was involved in the pathological processes of hepatocellular carcinoma through activation of the phosphatidylinositol 3-kinase/protein kinase B signaling pathway, which may provide an attractive potential diagnostic biomarker and therapeutic target for treatment of hepatocellular carcinoma.
A novel mutation (c.1093C > T; p.Arg365*) is described in a family with dizygotic twins with variable phenotype of Chudley-McCullough syndrome.
This mutation is predicted to abolish all four GoLoco domains in GPSM2 and this explains the bioinformatic prediction for this mutation to be functionally damaging. Full clinical and molecular accounts of the novel mutation are provided in this paper.
Kinocilium is essential for proper localization of Lgn, as well as Gai and aPKC, suggesting that cilium function plays a role in positioning of apical proteins critical for hearing.
This study determined the crystallographic structure of human Afadin in complex with LGN.
results fit a model whereby LGN influences interphase microtubule dynamics in endothelial cells to regulate migration, cell adhesion, and sprout extension, and reveal a novel non-mitotic role for LGN in sprouting angiogenesis
A crystal structure of Frmpd4-bound LGN in an oxidized form is also reported, although oxidation does not appear to strongly affect the interaction with Frmpd4.
LGN is required for mitotic spindle rotation but not orientation maintenance.
Hepatocyte Par1b defines lumen position in concert with the position of the astral microtubule anchoring complex LGN-NuMA to yield the distinct epithelial division phenotypes.
one homozygous frameshift GPSM2 variants c.1473delG was identified in three Chudley-McCullough syndrome Dutch patients.
Data indicate that dynein- and astral microtubule-mediated transport of Galphai/LGN/nuclear mitotic apparatus (NuMA) complex from cell cortex to spindle poles.
Studies indicate that the Inscuteable (Insc)and NuMA are mutually exclusive interactors of LGN.
Results show compound heterozygous mutations in the GPSM2 gene, in affected members of a family with Chudley-McCullough syndrome, co-segregate in the family as an autosomal recessive trait.
Overexpression of LGN decreases the activity of cellular sGC, whereas knockdown of LGN mRNA and protein correlated with increased sGC activity
GPSM2 is required for orienting the mitotic spindle during cell division in multiple tissues, suggesting that the sensorineural hearing loss and characteristic brain malformations of CMS are due to defects in asymmetric cell divisions during development
Mutation of the mouse orthologue of GPSM2 affects actin-rich stereocilia elongation in auditory and vestibular hair cells, causing deafness and balance defects. Gpsm2 defines an approximately 200 nm nanodomain at the tips of stereocilia and this localization requires the presence of Galphai3, myosin 15 and whirlin. Loss of Gpsm2 leads to decreased outgrowth and a disruption of actin dynamics in neuronal growth cones.
LGN in complex with the asymmetric domain of Inscuteable, which reveals a tetrameric arrangement of intertwined molecules.
LGN and Galphai participate in a long-inferred signal that originates outside the bundle to model its staircase-like architecture, a property that is essential for direction sensitivity to mechanical deflection and hearing.
these results show a context-dependent function for LGN.
support for the hitherto untested model that Par3-mInsc and Galphai3 act cooperatively to polarize LGN and promote perpendicular divisions
LGN-TPR motifs are versatile and capable of recognizing multiple targets via diverse binding modes.
X-ray crystallography and binding studies reveal that LGN GoLoco binding motifs are potent guanine nucleotide dissociation inhibitors.
The restricted localization of NuMA in the lateral belt is instructive for the planar alignment of the mitotic spindle, and required for its planar maintenance.
Knocking out LGN, (the G protein regulator), randomized the orientation of normally planar neuroepithelial divisions.
The primary aim of this study was to determine the spatial distribution and time course of mouse homolog of Drosophila Partner of Inscuteable (mPins) expression in the developing and adult mouse eye.
Excessive LGN induces meiotic spindle organization defects by elongating the spindle and enhancing pole focusing, whereas depletion of LGN by RNA interference results in meiotic spindle deformation and chromosome misalignment.
The protein encoded by this gene belongs to a family of proteins that modulate activation of G proteins, which transduce extracellular signals received by cell surface receptors into integrated cellular responses. The N-terminal half of this protein contains 10 copies of leu-gly-asn (LGN) repeat, and the C-terminal half contains 4 GoLoco motifs, which are involved in guanine nucleotide exchange. This protein may play a role in neuroblast division and in the development of normal hearing. Mutations in this gene are associated with autosomal recessive nonsyndromic deafness (DFNB82).
G-protein signalling modulator 2 (AGS3-like, C. elegans)
, G-protein-signaling modulator 2
, mosaic protein LGN
, G-protein signaling modulator 2 (AGS3-like, C. elegans)
, G-protein signaling modulator 2 (AGS3-like)
, LGN protein
, pins homolog (Drosophia)