Nuclear responses of WCCB TBM with different container designs

2020 ◽  
Vol 157 ◽  
pp. 111672
Author(s):  
Hyoseong Gwon ◽  
Wenhai Guan ◽  
Kentaro Hattori ◽  
Hiromasa Iida ◽  
Hisashi Tanigawa ◽  
...  
Keyword(s):  
Nuclear Responses

scholarly journals Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun.

1994 ◽  
Vol 14 (11) ◽  
pp. 7352-7362 ◽  
Author(s):  
E Cano ◽  
C A Hazzalin ◽  
L C Mahadevan
Keyword(s):  
Protein Kinases ◽  
Map Kinases ◽  
Early Gene ◽  
Intracellular Signals ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Serine Kinases ◽  
Translational Arrest ◽  
Epidermal Growth ◽  
Nuclear Responses

Independent of its ability to block translation, anisomycin intrinsically initiates intracellular signals and immediate-early gene induction [L. C. Mahadevan and D. R. Edwards, Nature (London) 349:747-749, 1991]. Here, we characterize further its action as a potent, selective signalling agonist. In-gel kinase assays show that epidermal growth factor (EGF) transiently activates five kinases: the mitogen-activated protein (MAP) kinases ERK-1 and -2, and three others, p45, p55, and p80. Anisomycin, at inhibitory and subinhibitory concentrations, does not activate ERK-1 and -2 but elicits strong sustained activation of p45 and p55, which are unique in being serine kinases whose detection is enhanced with poly-Glu/Tyr or poly-Glu/Phe copolymerized in these gels. Translational arrest using emetine or puromycin does not activate p45 and p55 but does prolong EGF-stimulated ERK-1 and -2 activation. Rapamycin, which blocks anisomycin-stimulated p70/85S6k activation without affecting nuclear responses, has no effect on p45 or p55 kinase. p45 and p55 are activable by okadaic acid or UV irradiation, and both kinases phosphorylate the c-Jun NH2-terminal peptide 1-79, putatively placing them within c-Jun NH2-terminal kinase/stress-activated protein kinase (JNK/SAPK) subfamily of MAP kinases. Thus, the EGF- and anisomycin-activated kinases p45 and p55 are strongly implicated in signalling to c-fos and c-jun, whereas the MAP kinases ERK-1 and -2 are not essential for this process.

Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun

1994 ◽  
Vol 14 (11) ◽  
pp. 7352-7362 ◽  
Author(s):  
E Cano ◽  
C A Hazzalin ◽  
L C Mahadevan
Keyword(s):  
Protein Kinases ◽  
Map Kinases ◽  
Early Gene ◽  
Intracellular Signals ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Serine Kinases ◽  
Translational Arrest ◽  
Epidermal Growth ◽  
Nuclear Responses

Independent of its ability to block translation, anisomycin intrinsically initiates intracellular signals and immediate-early gene induction [L. C. Mahadevan and D. R. Edwards, Nature (London) 349:747-749, 1991]. Here, we characterize further its action as a potent, selective signalling agonist. In-gel kinase assays show that epidermal growth factor (EGF) transiently activates five kinases: the mitogen-activated protein (MAP) kinases ERK-1 and -2, and three others, p45, p55, and p80. Anisomycin, at inhibitory and subinhibitory concentrations, does not activate ERK-1 and -2 but elicits strong sustained activation of p45 and p55, which are unique in being serine kinases whose detection is enhanced with poly-Glu/Tyr or poly-Glu/Phe copolymerized in these gels. Translational arrest using emetine or puromycin does not activate p45 and p55 but does prolong EGF-stimulated ERK-1 and -2 activation. Rapamycin, which blocks anisomycin-stimulated p70/85S6k activation without affecting nuclear responses, has no effect on p45 or p55 kinase. p45 and p55 are activable by okadaic acid or UV irradiation, and both kinases phosphorylate the c-Jun NH2-terminal peptide 1-79, putatively placing them within c-Jun NH2-terminal kinase/stress-activated protein kinase (JNK/SAPK) subfamily of MAP kinases. Thus, the EGF- and anisomycin-activated kinases p45 and p55 are strongly implicated in signalling to c-fos and c-jun, whereas the MAP kinases ERK-1 and -2 are not essential for this process.

Rapid Nuclear Responses to Action Potentials

2006 ◽  
pp. 401-418
Author(s):  
J. Paige Adams ◽  
Eric Hudgins ◽  
Joseph J. Lundquist ◽  
Meilan Zhao ◽  
Serena M. Dudek
Keyword(s):  
Action Potentials ◽  
Nuclear Responses

scholarly journals Retrograde Control of Cytosolic Translation Targets Synthesis of Plastid Localized Proteins and Nuclear Responses for Efficient Light Acclimation

2021 ◽  
Author(s):  
Marten Moore ◽  
Aaron Smith ◽  
Corinna Wesemann ◽  
Sonja Schmidtpott ◽  
Melanie Wegener ◽  
...  
Keyword(s):  
Transcriptional Response ◽  
Transcript Abundance ◽  
Protein Translation ◽  
Retrograde Signaling ◽  
Just In Time ◽  
Protein Accumulation ◽  
Translation Efficiency ◽  
Multiple Components ◽  
Associated Proteins ◽  
Nuclear Responses

AbstractCanonical retrograde signaling is the transmission of information from organelles to the nucleus. Discrepancies between protein accumulation and transcript abundance in response to oxidative stress were suggestive of protein translation responding to retrograde signaling. Here we uncover multiple components of a translation-dependent retrograde signaling pathway that impact translation efficiency and gene expression, including the kinases, MPK6 and the SnRK1 subunit, AKIN10. Global ribosome foot-printing demonstrated rapid differential loading of 939 of transcripts from polyribosomes within 10 min after transfer from Low to High-light. Translationally regulated transcripts shared motifs in their 5’-UTR that act as binding sites for RBPs such as GAPC. The Stress Associated Proteins 2 and 3 carry such motifs in their UTRs and interact with the calcium sensor Calmodulin-like 49, relocating to the nucleus to co-regulate a translation-dependent transcriptional response. Translation dependent retrograde signaling bifurcates into a direct translational circuit and a translation-reliant nuclear circuit synchronizing translation, nuclear and anterograde response pathways, which may serve as a just in time-provision of needed proteins to the plastids.

scholarly journals A Micropatterning Strategy to Study Nuclear Mechanotransduction in Cells

Micromachines ◽  
2019 ◽  
Vol 10 (12) ◽  
pp. 810 ◽  
Author(s):  
Markville Bautista ◽  
Anthony Fernandez ◽  
Fabien Pinaud
Keyword(s):  
Nuclear Envelope ◽  
Microcontact Printing ◽  
Skin Fibroblasts ◽  
Endoplasmic Reticulum Membrane ◽  
Wild Type ◽  
Network Cell ◽  
Cell Micropatterning ◽  
Nuclear Responses ◽  
Cell Adhesion And Proliferation

Micropatterning techniques have been widely used in biology, particularly in studies involving cell adhesion and proliferation on different substrates. Cell micropatterning approaches are also increasingly employed as in vitro tools to investigate intracellular mechanotransduction processes. In this report, we examined how modulating cellular shapes on two-dimensional rectangular fibronectin micropatterns of different widths influences nuclear mechanotransduction mediated by emerin, a nuclear envelope protein implicated in Emery–Dreifuss muscular dystrophy (EDMD). Fibronectin microcontact printing was tested onto glass coverslips functionalized with three different silane reagents (hexamethyldisilazane (HMDS), (3-Aminopropyl)triethoxysilane (APTES) and (3-Glycidyloxypropyl)trimethoxysilane (GPTMS)) using a vapor-phase deposition method. We observed that HMDS provides the most reliable printing surface for cell micropatterning, notably because it forms a hydrophobic organosilane monolayer that favors the retainment of surface antifouling agents on the coverslips. We showed that, under specific mechanical cues, emerin-null human skin fibroblasts display a significantly more deformed nucleus than skin fibroblasts expressing wild type emerin, indicating that emerin plays a crucial role in nuclear adaptability to mechanical stresses. We further showed that proper nuclear responses to forces involve a significant relocation of emerin from the inner nuclear envelope towards the outer nuclear envelope and the endoplasmic reticulum membrane network. Cell micropatterning by fibronectin microcontact printing directly on HMDS-treated glass represents a simple approach to apply steady-state biophysical cues to cells and study their specific mechanobiology responses in vitro.

scholarly journals Magnetic HexadecapoleγTransitions and Neutrino-Nuclear Responses in Medium-Heavy Nuclei

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Lotta Jokiniemi ◽  
Jouni Suhonen ◽  
Hiroyasu Ejiri
Keyword(s):  
Nuclear Matrix ◽  
Wave Functions ◽  
Matrix Elements ◽  
Heavy Nuclei ◽  
Magnetic Quadrupole ◽  
Order Of Magnitude ◽  
Nuclear Responses ◽  
Beta Decays ◽  
Gamow Teller ◽  
Phonon Model

Neutrino-nuclear responses in the form of squares of nuclear matrix elements, NMEs, are crucial for studies of neutrino-induced processes in nuclei. In this work we investigate magnetic hexadecapole (M4) NMEs in medium-heavy nuclei. The experimentally derived NMEs,MEXP(M4), deduced from observed M4γtransition half-lives are compared with the single-quasiparticle (QP) NMEs,MQP(M4), and the microscopic quasiparticle-phonon model (MQPM) NMEsMMQPM(M4). The experimentally derived M4 NMEs are found to be reduced by a coefficientk≈0.29with respect toMQP(M4) and byk≈0.33with respect toMMQPM(M4). The M4 NMEs are reduced a little by the quasiparticle-phonon correlations of the MQPM wave functions but mainly by other nucleonic and nonnucleonic correlations which are not explicitly included in the MQPM. The found reduction rates are of the same order of magnitude as those for magnetic quadrupoleγtransitions and Gamow-Teller (GT) and spin-dipole (SD)βtransitions. The impacts of the found reduction coefficients on the magnitudes of the NMEs involved in astroneutrino interactions and neutrinoless double beta decays are discussed.

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