Coordinated interactions between actin and microtubules through crosslinkers in neurite retraction induced by lysophosphatidic acid

Fukushima, Nobuyuki; Furuta, Daisuke; Tsujiuchi, Toshifumi

doi:10.1016/j.neuint.2011.04.020

Cited by 11 publications

(8 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed, LPA has been identified to primarily influence GSK3β-mediated rearrangement of microfilaments (MFs) and polymerization-dependent microtubules (MTs). Such interactions between MF-MT have been indicated to regulate LPA-induced neurite outgrowth (Fukushima and Morita, 2006;Fukushima et al, 2011). In this regard, conclusions can be drawn that LPA-mediated G 12/13 activation increases RhoA GTPase activity, thus leading to the upregulation of GSK-3, downstream disorganization of MTs, growth cone collapse as well as the retraction of neurites (Sayas et al, 1999).…”

Section: Lpa and Neuronal Differentiationmentioning

confidence: 99%

Lysophospholipids and Their G-Coupled Protein Signaling in Alzheimer’s Disease: From Physiological Performance to Pathological Impairment

Hao

Guo

Feng

et al. 2020

Front. Mol. Neurosci.

View full text Add to dashboard Cite

Lysophospholipids (LPLs) are bioactive signaling lipids that are generated from phospholipase-mediated hydrolyzation of membrane phospholipids (PLs) and sphingolipids (SLs). Lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) are two of the best-characterized LPLs which mediate a variety of cellular physiological responses via specific G-protein coupled receptor (GPCR) mediated signaling pathways. Considerable evidence now demonstrates the crucial role of LPA and S1P in neurodegenerative diseases, especially in Alzheimer's disease (AD). Dysfunction of LPA and S1P metabolism can lead to aberrant accumulation of amyloid-β (Aβ) peptides, the formation of neurofibrillary tangles (NFTs), neuroinflammation and ultimately neuronal death. Summarizing LPA and S1P signaling profile may aid in profound health and pathological processes. In the current review, we will introduce the metabolism as well as the physiological roles of LPA and S1P in maintaining the normal functions of the nervous system. Given these pivotal functions, we will further discuss the role of dysregulation of LPA and S1P in promoting AD pathogenesis.

show abstract

Section: Lpa and Neuronal Differentiationmentioning

confidence: 99%

Lysophospholipids and Their G-Coupled Protein Signaling in Alzheimer’s Disease: From Physiological Performance to Pathological Impairment

Hao

Guo

Feng

et al. 2020

Front. Mol. Neurosci.

View full text Add to dashboard Cite

show abstract

“…Multiple cellular responses have been reported for this bioactive natural lipid in the central nervous system (CNS) as well as in neural cell lines. LPA elicited sharp changes in cell’s shape and morphology, growth cone collapse and neurite retraction in many neuronal cell lines through activation of the small GTPase Rho which in turn contracts cytoskeleton (Ye et al, 2002 ; Choi et al, 2010 ; Fukushima et al, 2011 ). Furthermore, LPA also affect cell motility in glioma cell lines through Rho/Rho-associated kinases (ROKC) signaling cascades, which may contribute to their invasive phenotype in vivo (Manning et al, 2000 ).…”

Section: Introductionmentioning

confidence: 99%

Glutaminase and MMP-9 Downregulation in Cortex and Hippocampus of LPA1 Receptor Null Mice Correlate with Altered Dendritic Spine Plasticity

Peñalver

Campos-Sandoval

Blanco

et al. 2017

Front. Mol. Neurosci.

View full text Add to dashboard Cite

Lysophosphatidic acid (LPA) is an extracellular lipid mediator that regulates nervous system development and functions acting through G protein-coupled receptors (GPCRs). Here we explore the crosstalk between LPA1 receptor and glutamatergic transmission by examining expression of glutaminase (GA) isoforms in different brain areas isolated from wild-type (WT) and KOLPA1 mice. Silencing of LPA1 receptor induced a severe down-regulation of Gls-encoded long glutaminase protein variant (KGA) (glutaminase gene encoding the kidney-type isoforms, GLS) protein expression in several brain regions, particularly in brain cortex and hippocampus. Immunohistochemical assessment of protein levels for the second type of glutaminase (GA) isoform, glutaminase gene encoding the liver-type isoforms (GLS2), did not detect substantial differences with regard to WT animals. The regional mRNA levels of GLS were determined by real time RT-PCR and did not show significant variations, except for prefrontal and motor cortex values which clearly diminished in KO mice. Total GA activity was also significantly reduced in prefrontal and motor cortex, but remained essentially unchanged in the hippocampus and rest of brain regions examined, suggesting activation of genetic compensatory mechanisms and/or post-translational modifications to compensate for KGA protein deficit. Remarkably, Golgi staining of hippocampal regions showed an altered morphology of glutamatergic pyramidal cells dendritic spines towards a less mature filopodia-like phenotype, as compared with WT littermates. This structural change correlated with a strong decrease of active matrix-metalloproteinase (MMP) 9 in cerebral cortex and hippocampus of KOLPA1 mice. Taken together, these results demonstrate that LPA signaling through LPA1 influence expression of the main isoenzyme of glutamate biosynthesis with strong repercussions on dendritic spines maturation, which may partially explain the cognitive and learning defects previously reported for this colony of KOLPA1 mice.

show abstract

“…We considered a role for drebrin among the host of proteins which have the potential to directly bind both the axonal actin filament and microtubule cytoskeleton (Houseweart and Cleveland, 1999; Dent and Gertler, 2003; Rodriguez et al, 2003; Goryunov et al, 2010; Fukushima et al, 2011; Huber et al, 2014; Villarroel-Campos D and Gonzalez-Billault, 2014). Drebrin is a neuronally expressed actin filament binding protein that has been involved in the regulation of neuronal morphology (Dun and Chilton, 2010; Dun et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Drebrin coordinates the actin and microtubule cytoskeleton during the initiation of axon collateral branches

Ketschek

Spillane

Dun

et al. 2016

Developmental Neurobiology

View full text Add to dashboard Cite

Drebrin is a cytoskeleton-associated protein which can interact with both actin filaments and the tips of microtubules. Its roles have been studied mostly in dendrites, and the functions of drebrin in axons are less well understood. In this work we analyzed the role of drebrin, through shRNA-mediated depletion and over-expression, in the collateral branching of chicken embryonic sensory axons. We report that drebrin promotes the formation of axonal filopodia and collateral branches in vivo and in vitro. Live imaging of cytoskeletal dynamics revealed that drebrin promotes the formation of filopodia from precursor structures termed axonal actin patches. Endogenous drebrin localizes to actin patches and depletion studies indicate that drebrin contributes to the development of patches. In filopodia, endogenous drebrin localizes to the proximal portion of the filopodium. Drebrin was found to promote the stability of axonal filopodia and the entry of microtubule plus tips into axonal filopodia. The effects of drebrin on the stabilization of filopodia are independent of its effects on promoting microtubule targeting to filopodia. Inhibition of myosin II induces a redistribution of endogenous drebrin distally into filopodia, and further increases branching in drebrin overexpressing neurons. Finally, a 30 minute treatment with the branch inducing signal nerve growth factor increases the levels of axonal drebrin. The current study determines the specific roles of drebrin in the regulation of the axonal cytoskeleton, and provides evidence that drebrin contributes to the coordination of the actin and microtubule cytoskeleton during the initial stages of axon branching.

show abstract

Coordinated interactions between actin and microtubules through crosslinkers in neurite retraction induced by lysophosphatidic acid

Cited by 11 publications

References 33 publications

Lysophospholipids and Their G-Coupled Protein Signaling in Alzheimer’s Disease: From Physiological Performance to Pathological Impairment

Lysophospholipids and Their G-Coupled Protein Signaling in Alzheimer’s Disease: From Physiological Performance to Pathological Impairment

Glutaminase and MMP-9 Downregulation in Cortex and Hippocampus of LPA1 Receptor Null Mice Correlate with Altered Dendritic Spine Plasticity

Drebrin coordinates the actin and microtubule cytoskeleton during the initiation of axon collateral branches

Contact Info

Product

Resources

About