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Study shows that modulation of matrix pore size or of lamin A expression known to modulate nuclear stiffness directly impinges on levels of MT1-MMP-mediated pericellular collagenolysis by cancer cells. This response requires an intact connection between the nucleus and the centrosome via the linker of nucleoskeleton and cytoskeleton (LINC) complex protein nesprin-2 and dynein adaptor Lis1.
Platelet-activating factor increases reactive oxygen species-mediated microbicidal activity of human macrophages infected with Leishmania braziliensis.
LIS1 promotes dynactin-dependent tracking of dynein on both growing and shrinking plus ends. LIS1 also increases the frequency and velocity of processive dynein movements that are activated by complex formation with dynactin and a cargo adaptor.
Microarray analysis after PAFAH1B1 knockdown and its overexpression indicated that the protein maintains Matrix Gla Protein expression
A novel recurrent LIS1 splice site mutation in classic lissencephaly have been found in two unrelated pediatric patients.
Lis1 has two opposing modes of regulating dynein, being capable of inducing both low and high affinity for the microtubule; study shows that these opposing modes depend on the stoichiometry of Lis1 binding to dynein and that this stoichiometry is regulated by the nucleotide state of dynein's AAA3 domain.
genetic variants in LIS1 may contribute to AML risk in Chinese population.
Val279Phe gene polymorphisms in PAF-AH are associated with PAF-AH activity and PAF and GMP-140 levels and may be a risk factor for Henoch-Schonlein purpura with gastrointestinal bleeding
There were no significant associations between R92H and A379V variants of PAF-AH gene and risk of polycystic ovary syndrome in Chinese women.
results indicate that the NAGK-dynein interaction with the involvements of Lis1 and NudE1 plays an important role in prophase nuclear envelope breakdown (NEB) and metaphase MT-KT attachment during eukaryotic cell division.
In testis: varied levels among samples of different spermatogenic abilities, protein expression restricted to spermatogonia, spermatocytes and spermatids. Also varied levels in unfertilized oocytes, zygotes, cleavage stage embryos and blastocysts.
Results showed that miR-144 was reduced in cholangiocarcinoma tissues and suggested that miR-144 may be an essential suppresser of cholangiocarcinoma cell proliferation and invasion through targeting LIS1.
LIS1 and TSNAX genes are not associated with susceptibility to bipolar I disorder in Chinese Han population.
Identify a key role for Lis1 in hematopoietic stem cells and mark its directed control of asymmetric division as a critical regulator of normal and malignant hematopoietic development
LIS1 gene duplication is associated with developmental, behavioral and brain abnormalities.
LIS1 is required for dynein-mediated transport induced by membrane tethering of BICD2-N and LIS1 contributes to dynein accumulation at microtubule plus ends and BICD2-positive cellular structures.
PAFAH1B1 overexpression contributes to lung tumorigenesis and poor prognosis.
Studies identified three genes, CHD5, PAFAH1B1, and NME1, strongly associated with patient outcome.
Studies indicate that binding of dynactin, LIS1 and NudEL regulate cytoplasmic dynein motor activity.
The results did not detect a significant association. It indicated that common genetic variations in LIS1 genes might not play a role in the genetic predisposition to autism.
genetic deletion of Lis1 in the mouse liver increases lipid accumulation and inflammation in this organ. Further analysis revealed that loss of Lis1 triggers endoplasmic reticulum (ER) stress and reduces triglyceride secretion.
Lis1 loss in the midbrain/hindbrain causes a severe phenotype. Brainstem regions known to house cardiorespiratory centers showed signs of axonal dysfunction in KO animals. Transport defects, neurofilament alterations, and varicosities were observed in axons in cultured dorsal root ganglia neurons from KO animals.
This study examined the effect of Pafah1b1 overexpression on radial migration of cerebral cortical neurons and found that enhanced expression of Pafah1b1 caused over-migration of neurons into the marginal zone, and Pafah1b1-overexpressing neurons that entered the marginal zone were disoriented.
Lis1 dysfunction reduces migration and traction force production in fibroblasts.
findings suggest that Lis1 is required for germinal center (GC) B cell expansion, affinity maturation, and maintaining functional intact GC response, thus ensuring both the quantity and quality of Ab response
Lis1 plays an important role in T cell homeostasis and the generation of memory T lymphocytes.
This study demonstrated that LIS-1 regulate the septohippocampal cholinergic projection developmental.
Lis1 is required for the expansion of FL-HSCs by ensuring their genomic stability and therefore promoting their survival.
Results show that LIS1 acts via the LIS1-NDEL1-dynein complex to regulate astral microtubule MT plus-ends dynamics and establish proper contacts of MTs with the cell cortex to ensure precise cell division.
Conditional deletion of Lis1 in the hematopoietic system led to a severe bloodless phenotype, depletion of the stem cell pool and embryonic lethality.
Rab6a mediates LIS1 release from a LIS1-dynein complex followed by dynein activation.
LIS1 plays prominently in filopodia dynamics and dendritic spine turnover.
Nde1 and Lis1 regulate central nervous system development by interpreting midline signals differentially.
Lis1 mediates planar polarity of auditory hair cells through regulation of microtubule organization.
We have investigated the mouse PAFAH1B subunit genes during brain development
Lis1 is required for the dorsally directed tangential migration of many sympathetic and parasympathetic preganglionic neurons and a subset of somatic motor neurons.
findings indicate that disruption of LIS1 has direct effects on excitatory synaptic transmission independent of laminar disorganization.
results indicate that LIS1 is a previously unrecognized regulator of osteoclast formation, microtubule organization, and lysosomal secretion by virtue of its ability to modulate dynein function and Plekhm1
A three-dimensional regulation of radial glial cells' cytoarchitecture by the Lis1-Nde1-DGC complex determines the number and spatial organization of cortical neurons as well as the size and shape of the cerebral cortex.
Lis1 overexpression stimulated retrograde transport in axons, while a Lis1 dynein-binding mutant severely disrupted transport.
Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis.
Full rescue by the coiled-coil domain requires LIS1 binding, and increasing LIS1 concentration partly rescues aster formation
PAFAH Ib phospholipase A2 subunits have distinct roles in maintaining Golgi structure and function.
Results suggest that LIS1 is essential to mediate genomic union in a process that involves the dynein-dynactin complex.
This locus was identified as encoding a gene that when mutated or lost caused the lissencephaly associated with Miller-Dieker lissencephaly syndrome. This gene encodes the non-catalytic alpha subunit of the intracellular Ib isoform of platelet-activating factor acteylhydrolase, a heterotrimeric enzyme that specifically catalyzes the removal of the acetyl group at the SN-2 position of platelet-activating factor (identified as 1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine). Two other isoforms of intracellular platelet-activating factor acetylhydrolase exist: one composed of multiple subunits, the other, a single subunit. In addition, a single-subunit isoform of this enzyme is found in serum.
, PAF acetylhydrolase 45 kDa subunit
, PAF-AH 45 kDa subunit
, PAF-AH alpha
, PAFAH alpha
, lissencephaly 1 protein
, lissencephaly-1 protein
, platelet-activating factor acetylhydrolase IB subunit alpha
, platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit (45kD)
, platelet-activating factor acetylhydrolase, isoform Ib, subunit 1 (45kDa)
, platelet-activating factor acetylhydrolase 1b, regulatory subunit 1
, platelet-activating factor acetylhydrolase, isoform 1b, beta1 subunit
, PAF-AH beta
, platelet-activating factor acetylhydrolase beta subunit (PAF-AH beta)
, platelet-activating factor acetylhydrolase, isoform 1b, subunit 1
, platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit 45kDa
, lissencephaly-1 homolog
, lissencephaly-1 homolog B
, platelet-activating factor acetylhydrolase Ib-alpha subunit
, Miller-Dieker syndrome chromosome region
, Lissencephaly-1 protein
, platelet-activating factor acetylhydrolase isoform Ib alpha subunit
, lissencephaly-1 homolog A
, platelet-activating factor acetylhydrolase IB subunit alpha a