Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides

Saarikangas, Juha; Zhao, Hongxia; Lappalainen, Pekka

doi:10.1152/physrev.00036.2009

Cited by 429 publications

(455 citation statements)

References 414 publications

(462 reference statements)

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“…(2) Cell adhesion molecules: N-cadherin has been reported to be asymmetrically distributed during early neuronal development, in one of the earliest events during the establishment of asymmetry [48,72]. (3) Phosphorylated derivatives of the phospholipid phosphatidylinositol or phosphoinositides: as membrane-localized signaling molecules which interact with the actin cytoskeleton [73,74], PIP3, a member of this family, has been shown to promote neuronal polarization [75,76] and the formation of axonal filopodia [77].…”

Section: Discussionmentioning

confidence: 99%

Actin Aggregations Mark the Sites of Neurite Initiation

et al. 2016

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A salient feature of neurons is their intrinsic ability to grow and extend neurites, even in the absence of external cues. Compared to the later stages of neuronal development, such as neuronal polarization and dendrite morphogenesis, the early steps of neuritogenesis remain relatively unexplored. Here we showed that redistribution of cortical actin into large aggregates preceded neuritogenesis and determined the site of neurite initiation. Enhancing actin polymerization by jasplakinolide treatment effectively blocked actin redistribution and neurite initiation, while treatment with the actin depolymerizing agents latrunculin A or cytochalasin D accelerated neurite formation. Together, these results demonstrate a critical role of actin dynamics and reorganization in neurite initiation. Further experiments showed that microtubule dynamics and protein synthesis are not required for neurite initiation, but are required for later neurite stabilization. The redistribution of actin during early neuronal development was also observed in the cerebral cortex and hippocampus in vivo.

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Section: Discussionmentioning

confidence: 99%

Actin Aggregations Mark the Sites of Neurite Initiation

et al. 2016

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“…This pathway was described as being responsible for stimulating protein kinase (PK) activation, including mitogen-activated kinase protein (MAPK), which has been previously reported as an attendee in the regulation of oocyte meiotic resumption, in which it may act directly or indirectly [9]. Recent studies have shown that MAPK is required in gonadotropininduced meiotic resumption [35,38,39,44]. Other studies have also established that MAPK as well as protein kinase A (PKA) interrupts the communication between the CCs and the oocyte, thus decreasing the cyclic adenosine Fig.…”

Section: Discussionmentioning

confidence: 99%

“…4 Metabolic correlation between phosphatidylserine (PS) and phosphatidylethanolamine (PE), found in the non-pregnant group, and phosphatidylcholine (PC), found in the pregnant group. PSS1 PS synthase-1; PSS2 PS synthase-2; PSD phosphatidylserine decarboxylase; PEMT phosphatidylethanolamine N-methyltransferase; ET ethanolamine transferase; EK ethanolamine kinase; CPT phosphoethanolamine cytidylyltransferase; EPT ethanolamine phosphotransferase; CT ethanolamine transferase; CK choline kinase monophosphate (cAMP) level in the female gamete, which initiates its meiotic resumption [26,29,35]. Therefore, we propose that the high PI intensity in the NP group indicates that the degradation of DAG has been not occurring or that it has been occurring at low activity, due to the reduced efficiency of meiotic resumption in this group.…”

Section: Discussionmentioning

confidence: 99%

The follicular microenviroment as a predictor of pregnancy: MALDI-TOF MS lipid profile in cumulus cells

Montani

Cordeiro

Regiani

et al. 2012

J Assist Reprod Genet

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Purpose This research proposed to study the changes in lipid composition in cumulus cells (CCs) from women who achieved pregnancy compared with women who did not, after in vitro fertilization treatment. This approach has the potential to provide novel information on the lipid metabolism of the CCs and as an additional method to predict pregnancy. Method Fifty-four samples from couples with tubal and male factor infertility and where the female partner was age 35 or younger were divided in two groups according to their level of hCG 14 days after embryo transfer as follows: (1) 23 samples in pregnant group and (2) 31 samples in non-pregnant group. Lipid extraction was performed by the Bligh-Dyer protocol, and lipid profiles were obtained by MALDI-TOF MS. Mass spectra data were processed with MassLynx, and statistical analysis was performed using MarkerLynx extended statistic. OPLS-DA model was built. Results S-plot Analysis revealed three ions as potential markers in the pregnant group, and five ions in the nonpregnant group. These ions were identified in the human metabolome database (HMDB) as phosphatidylcholine in the pregnant group and as phosphatidylethanolamine, phosphatidylserine and phosphatidylinositol species in the non-pregnant group. These lipids might be involved in cell proliferation and differentiation, apoptosis and GAP junction regulation. Conclusion We conclude that MALDI-TOF MS can be used as an informative and fast analytical strategy to obtain and study the lipid profile of cumulus cells and can potentially be used as a supporting tool to predict pregnancy based on the metabolic state of the CCs.

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Section: -Conclusionmentioning

confidence: 99%

“…In turn, this may induce segregation of PIP 2 in membranes. Given the importance of this lipid in actin dynamics (for review see [87]), ERM-induced PIP 2 clustering may reveal to be of high physiological importance.At this stage, it is clear that membrane binding triggers conformational changes in ERM. Does this conformational change permit ERM interaction with actin and what is the part of phosphorylation in this process?…”

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confidence: 99%

Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin

2013

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Ezrin, radixin and moesin (ERM) proteins are now more and more recognized to play a key role in a large number of important physiological processes such as morphogenesis, cancer metastasis and virus infection. Several recent reviews extensively discuss their biological functions [1][2][3][4]. In this review, we will first remind the main features of this family of proteins, which are now known as linkers and regulators of the plasma membrane/cytoskeleton linkage. We will then briefly review their implication in pathological processes such as cancer and viral infection. In a second part, we will focus on biochemical and biophysical approaches to study ERM interaction with lipid membranes and conformational change in well-defined environments. In vitro studies using biomimetic lipid membranes, especially large unilamellar vesicles (LUVs), giant unilamellar vesicles (GUVs) and supported lipid bilayers (SLBs) and recombinant proteins help to understand the molecular mechanism of conformational activation of ERM proteins. These tools are aimed to decorticate the different steps of the interaction, to simplify the experiments performed in vivo in much more complex biological environments. KeywordsEzrin; radixin and moesin; biomimetic membranes; phosphoinositol (4,5)-bisphosphate (PIP 2 ); large unilamellar vesicles; supported lipid bilayers; giant unilamelar vesicles Corresponding author: Catherine Picart, CNRS UMR 5628 (LMGP), Grenoble Institute of Technology and CNRS, 3 parvis Louis Néel, F-38016 Grenoble Cedex, France. Europe PMC Funders GroupAuthor Manuscript Biochimie. Author manuscript; available in PMC 2014 July 28. Published in final edited form as:Biochimie. 2013 January ; 95(1): 3-11. doi:10.1016/j.biochi.2012.09.033. Europe PMC Funders Author ManuscriptsEurope PMC Funders Author Manuscripts Biological importance of Ezrin, Radixin and Moesin General overview of ERM proteins (Ezrin, Radixin, Moesin)ERM proteins are localized at the plasma membrane in actin-rich surface structures (Fig 1) [5], such as microvilli, membrane ruffles, and lamellipodia in gut cells, lymphocytes, hepatocytes, spermatozoids, fibroblasts and in a variety of other cell types [5][6][7][8][9]. They are involved in various physiological processes including establishment of cell polarity, cell motility and cell signaling [10]. They act as linkers between the plasma membrane and the cortical actin cytoskeleton. From a structural point of view, ERMs are constituted of 3 domains : a membrane binding domain, also known as FERM (for band 4.1 protein, ezrin, radixin and moesin), and intermediary region and a actin binding domain called C-ERMAD (for C-terminal ERM-association domain) (Fig 2A).The FERM domain, constituted of ~300 amino acids, is characteristic of the proteins of the band 4.1 superfamily. These proteins also present other types of domains, including PDZ, tyrosine phosphatase, SH2-like, tyrosine kinase, kinase-like, myosin head, and PH domains [11]. In ERM proteins, the FERM domain is followed by a long α-helical region, whi...

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Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides

Cited by 429 publications

References 414 publications

Actin Aggregations Mark the Sites of Neurite Initiation

Actin Aggregations Mark the Sites of Neurite Initiation

The follicular microenviroment as a predictor of pregnancy: MALDI-TOF MS lipid profile in cumulus cells

Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin

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