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The protein encoded by GPSM2 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. Additionally we are shipping GPSM2 Antibodies (55) and GPSM2 Proteins (4) and many more products for this protein.
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 (show MLLT4 ELISA Kits) 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 (show FRMPD4 ELISA Kits)-bound LGN in an oxidized form is also reported, although oxidation does not appear to strongly affect the interaction with Frmpd4 (show FRMPD4 ELISA Kits).
LGN is required for mitotic spindle rotation but not orientation maintenance.
Hepatocyte Par1b (show MARK2 ELISA Kits) defines lumen position in concert with the position of the astral microtubule anchoring complex LGN-NuMA (show NUMA1 ELISA Kits) 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 (show NUMA1 ELISA Kits)) complex from cell cortex to spindle poles.
Studies indicate that the Inscuteable (Insc)and NuMA (show NUMA1 ELISA Kits) are mutually exclusive interactors of LGN.
these results show a context-dependent function for LGN.
support for the hitherto untested model that Par3 (show F2RL2 ELISA Kits)-mInsc and Galphai3 (show GNAI3 ELISA Kits) 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 (show NUMA1 ELISA Kits) 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.
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)