scholarly journals Coupled scRNA-Seq and Intracellular Protein Activity Reveal an Immunosuppressive Role of TREM2 in Cancer

Cell ◽  
2020 ◽  
Vol 182 (4) ◽  
pp. 872-885.e19 ◽  
Author(s):  
Yonatan Katzenelenbogen ◽  
Fadi Sheban ◽  
Adam Yalin ◽  
Ido Yofe ◽  
Dmitry Svetlichnyy ◽  
...  
Keyword(s):  
Intracellular Protein ◽  
Protein Activity

scholarly journals Molecular Genetic Evidence for the Role of SGT1 in the Intramolecular Complementation of Bs2 Protein Activity in Nicotiana benthamiana

2005 ◽  
Vol 17 (4) ◽  
pp. 1268-1278 ◽  
Author(s):  
R. Todd Leister ◽  
Douglas Dahlbeck ◽  
Brad Day ◽  
Yi Li ◽  
Olga Chesnokova ◽  
...  
Keyword(s):  
Nicotiana Benthamiana ◽  
Molecular Genetic ◽  
Genetic Evidence ◽  
Protein Activity ◽  
Molecular Genetic Evidence

scholarly journals Novel role of the muskelin–RanBP9 complex as a nucleocytoplasmic mediator of cell morphology regulation

2008 ◽  
Vol 182 (4) ◽  
pp. 727-739 ◽  
Author(s):  
Manojkumar Valiyaveettil ◽  
Amber A. Bentley ◽  
Priya Gursahaney ◽  
Rajaa Hussien ◽  
Ritu Chakravarti ◽  
...  
Keyword(s):  
Cell Morphology ◽  
Subcellular Fractionation ◽  
Cytoplasmic Localization ◽  
Intracellular Protein ◽  
Morphological Alterations ◽  
C Terminus ◽  
Evolutionarily Conserved ◽  
The Status ◽  
Interfering Rna

The evolutionarily conserved kelch-repeat protein muskelin was identified as an intracellular mediator of cell spreading. We discovered that its morphological activity is controlled by association with RanBP9/RanBPM, a protein involved in transmembrane signaling and a conserved intracellular protein complex. By subcellular fractionation, endogenous muskelin is present in both the nucleus and the cytosol. Muskelin subcellular localization is coregulated by its C terminus, which provides a cytoplasmic restraint and also controls the interaction of muskelin with RanBP9, and its atypical lissencephaly-1 homology motif, which has a nuclear localization activity which is regulated by the status of the C terminus. Transient or stable short interfering RNA–based knockdown of muskelin resulted in protrusive cell morphologies with enlarged cell perimeters. Morphology was specifically restored by complementary DNAs encoding forms of muskelin with full activity of the C terminus for cytoplasmic localization and RanBP9 binding. Knockdown of RanBP9 resulted in equivalent morphological alterations. These novel findings identify a role for muskelin–RanBP9 complex in pathways that integrate cell morphology regulation and nucleocytoplasmic communication.

Structural chemistry involved in information detection and transmission by gas sensor heme proteins: Resonance Raman investigation

2008 ◽  
Vol 80 (12) ◽  
pp. 2667-2678 ◽  
Author(s):  
Samir F. El-Mashtoly ◽  
Teizo Kitagawa
Keyword(s):  
Gas Sensor ◽  
Structural Changes ◽  
Catalytic Domain ◽  
Signal Transmission ◽  
Resonance Raman ◽  
Protein Activity ◽  
Sensor Proteins ◽  
Vinyl Group ◽  
Protein Moiety

A variety of heme-containing gas sensor proteins have been discovered by gene analysis from bacteria to mammals. In general, these proteins are composed of an N-terminal heme-containing sensor domain and a C-terminal catalytic domain. Binding of O2, CO, or NO to the heme causes a change in the structure of heme, which alters the protein conformation in the vicinity of the heme, and the conformational change is propagated to the catalytic domain, leading to regulation of the protein activity. This mini-review summarizes the recent resonance Raman studies obtained with both visible and UV excitation sources for two O2 sensor proteins, EcDOS and HemAT-Bs. These investigations have shown the role of heme propionate hydrogen-bonding interactions in communicating the heme structural changes, which occur upon ligand binding, from heme to the protein moiety. Furthermore, it is deduced that the contact interactions between the heme 2-vinyl group and the surrounding residues are also important for signal transmission from heme to protein in EcDOS.

scholarly journals Emerging roles of non-coding RNAs in vector-borne infections

2020 ◽  
Vol 134 (5) ◽  
pp. jcs246744
Author(s):  
Chaima Bensaoud ◽  
Larissa Almeida Martins ◽  
Hajer Aounallah ◽  
Michael Hackenberg ◽  
Michail Kotsyfakis
Keyword(s):  
Protein Activity ◽  
Arthropod Vector ◽  
Vector Borne Diseases ◽  
Defense Systems ◽  
Sequencing Studies ◽  
Vector Borne ◽  
Vertebrate Hosts ◽  
Non Coding Rnas ◽  
Eukaryotic Genomes

ABSTRACTNon-coding RNAs (ncRNAs) are nucleotide sequences that are known to assume regulatory roles previously thought to be reserved for proteins. Their functions include the regulation of protein activity and localization and the organization of subcellular structures. Sequencing studies have now identified thousands of ncRNAs encoded within the prokaryotic and eukaryotic genomes, leading to advances in several fields including parasitology. ncRNAs play major roles in several aspects of vector–host–pathogen interactions. Arthropod vector ncRNAs are secreted through extracellular vesicles into vertebrate hosts to counteract host defense systems and ensure arthropod survival. Conversely, hosts can use specific ncRNAs as one of several strategies to overcome arthropod vector invasion. In addition, pathogens transmitted through vector saliva into vertebrate hosts also possess ncRNAs thought to contribute to their pathogenicity. Recent studies have addressed ncRNAs in vectors or vertebrate hosts, with relatively few studies investigating the role of ncRNAs derived from pathogens and their involvement in establishing infections, especially in the context of vector-borne diseases. This Review summarizes recent data focusing on pathogen-derived ncRNAs and their role in modulating the cellular responses that favor pathogen survival in the vertebrate host and the arthropod vector, as well as host ncRNAs that interact with vector-borne pathogens.

Mitochondrial SIRT5 is present in follicular cells and is altered by reduced ovarian reserve and advanced maternal age

2014 ◽  
Vol 26 (8) ◽  
pp. 1072 ◽  
Author(s):  
Leanne Pacella-Ince ◽  
Deirdre L. Zander-Fox ◽  
Michelle Lane
Keyword(s):  
Follicular Fluid ◽  
Ovarian Reserve ◽  
Protein Function ◽  
Maternal Age ◽  
Cumulus Cells ◽  
Advanced Maternal Age ◽  
Oocyte Quality ◽  
Carbamoyl Phosphate ◽  
Protein Activity

Women with reduced ovarian reserve or advanced maternal age have an altered metabolic follicular microenvironment. As sirtuin 5 (SIRT5) senses cellular metabolic state and post-translationally alters protein function, its activity may directly impact on oocyte viability and pregnancy outcome. Therefore, we investigated the role of SIRT5 in relation to ovarian reserve and maternal age. Women (n = 47) undergoing routine IVF treatment were recruited and allocated to one of three cohorts based on ovarian reserve and maternal age. Surplus follicular fluid, granulosa and cumulus cells were collected. SIRT5 mRNA, protein and protein activity was confirmed in granulosa and cumulus cells via qPCR, immunohistochemistry, western blotting and desuccinylation activity. The presence of carbamoyl phosphate synthase I (CPS1), a target of SIRT5, was investigated by immunohistochemistry and follicular-fluid ammonium concentrations determined via microfluorometry. Women with reduced ovarian reserve or advanced maternal age had decreased SIRT5 mRNA, protein and desuccinylation activity in granulosa and cumulus cells resulting in an accumulation of follicular-fluid ammonium, presumably via alterations in activity of a SIRT5 target, CPS1, which was present in granulosa and cumulus cells. This suggests a role for SIRT5 in influencing oocyte quality and IVF outcomes.

scholarly journals SCL Assembles a Multifactorial Complex That Determines Glycophorin A Expression

2004 ◽  
Vol 24 (4) ◽  
pp. 1439-1452 ◽  
Author(s):  
Rachid Lahlil ◽  
Eric Lécuyer ◽  
Sabine Herblot ◽  
Trang Hoang
Keyword(s):  
Transcription Factors ◽  
Hematopoietic Cells ◽  
Inhibitory Effect ◽  
Erythroid Cell ◽  
Glycophorin A ◽  
Protein Activity ◽  
Protein Levels ◽  
Helix Loop Helix

ABSTRACT SCL/TAL1 is a hematopoietic-specific transcription factor of the basic helix-loop-helix (bHLH) family that is essential for erythropoiesis. Here we identify the erythroid cell-specific glycophorin A gene (GPA) as a target of SCL in primary hematopoietic cells and show that SCL occupies the GPA locus in vivo. GPA promoter activation is dependent on the assembly of a multifactorial complex containing SCL as well as ubiquitous (E47, Sp1, and Ldb1) and tissue-specific (LMO2 and GATA-1) transcription factors. In addition, our observations suggest functional specialization within this complex, as SCL provides its HLH protein interaction motif, GATA-1 exerts a DNA-tethering function through its binding to a critical GATA element in the GPA promoter, and E47 requires its N-terminal moiety (most likely entailing a transactivation function). Finally, endogenous GPA expression is disrupted in hematopoietic cells through the dominant-inhibitory effect of a truncated form of E47 (E47-bHLH) on E-protein activity or of FOG (Friend of GATA) on GATA activity or when LMO2 or Ldb-1 protein levels are decreased. Together, these observations reveal the functional complementarities of transcription factors within the SCL complex and the essential role of SCL as a nucleation factor within a higher-order complex required to activate gene GPA expression.

scholarly journals Uncoupling proteins in mitochondria of plants and some microorganisms.

2001 ◽  
Vol 48 (1) ◽  
pp. 145-155 ◽  
Author(s):  
W Jarmuszkiewicz
Keyword(s):  
Higher Plants ◽  
Uncoupling Protein ◽  
Physiological Role ◽  
Acanthamoeba Castellanii ◽  
Uncoupling Proteins ◽  
Protein Activity ◽  
Functional Connection ◽  
Mitochondrial Inner Membrane ◽  
Mitochondrial Carrier Family

Uncoupling proteins, members of the mitochondrial carrier family, are present in mitochondrial inner membrane and mediate free fatty acid-activated, purine-nucleotide-inhibited H+ re-uptake. Since 1995, it has been shown that the uncoupling protein is present in many higher plants and some microorganisms like non-photosynthetic amoeboid protozoon, Acanthamoeba castellanii and non-fermentative yeast Candida parapsilosis. In mitochondria of these organisms, uncoupling protein activity is revealed not only by stimulation of state 4 respiration by free fatty acids accompanied by decrease in membrane potential (these effects being partially released by ATP and GTP) but mainly by lowering ADP/O ratio during state 3 respiration. Plant and microorganism uncoupling proteins are able to divert very efficiently energy from oxidative phosphorylation, competing for deltamicroH+ with ATP synthase. Functional connection and physiological role of uncoupling protein and alternative oxidase, two main energy-dissipating systems in plant-type mitochondria, are discussed.

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