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      The Role of Cytoplasmic mRNA Cap-Binding Protein Complexes in Trypanosoma brucei and Other Trypanosomatids

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          Abstract

          Trypanosomatid protozoa are unusual eukaryotes that are well known for having unusual ways of controlling their gene expression. The lack of a refined mode of transcriptional control in these organisms is compensated by several post-transcriptional control mechanisms, such as control of mRNA turnover and selection of mRNA for translation, that may modulate protein synthesis in response to several environmental conditions found in different hosts. In other eukaryotes, selection of mRNA for translation is mediated by the complex eIF4F, a heterotrimeric protein complex composed by the subunits eIF4E, eIF4G, and eIF4A, where the eIF4E binds to the 5′-cap structure of mature mRNAs. In this review, we present and discuss the characteristics of six trypanosomatid eIF4E homologs and their associated proteins that form multiple eIF4F complexes. The existence of multiple eIF4F complexes in trypanosomatids evokes exquisite mechanisms for differential mRNA recognition for translation.

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          eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation.

          A Gingras, B Raught, N. Sonenberg (1999)
          Eukaryotic translation initiation factor 4F (eIF4F) is a protein complex that mediates recruitment of ribosomes to mRNA. This event is the rate-limiting step for translation under most circumstances and a primary target for translational control. Functions of the constituent proteins of eIF4F include recognition of the mRNA 5' cap structure (eIF4E), delivery of an RNA helicase to the 5' region (eIF4A), bridging of the mRNA and the ribosome (eIF4G), and circularization of the mRNA via interaction with poly(A)-binding protein (eIF4G). eIF4 activity is regulated by transcription, phosphorylation, inhibitory proteins, and proteolytic cleavage. Extracellular stimuli evoke changes in phosphorylation that influence eIF4F activity, especially through the phosphoinositide 3-kinase (PI3K) and Ras signaling pathways. Viral infection and cellular stresses also affect eIF4F function. The recent determination of the structure of eIF4E at atomic resolution has provided insight about how translation is initiated and regulated. Evidence suggests that eIF4F is also implicated in malignancy and apoptosis.
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            Stress granules: the Tao of RNA triage.

            Paul. Anderson, Nancy Kedersha (2008)
            Cytoplasmic RNA structures such as stress granules (SGs) and processing bodies (PBs) are functional byproducts of mRNA metabolism, sharing substrate mRNA, dynamic properties and many proteins, but also housing separate components and performing independent functions. Each can exist independently, but when coordinately induced they are often tethered together in a cytosolic dance. Although both self-assemble in response to stress-induced perturbations in translation, several recent reports reveal novel proteins and RNAs that are components of these structures but also perform other cellular functions. Proteins that mediate splicing, transcription, adhesion, signaling and development are all integrated with SG and PB assembly. Thus, these ephemeral bodies represent more than just the dynamic sorting of mRNA between translation and decay.
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              14-3-3 proteins: structure, function, and regulation.

              H. Fu, R. R. Subramanian, S. Masters (2000)
              The 14-3-3 proteins are a family of conserved regulatory molecules expressed in all eukaryotic cells. A striking feature of the 14-3-3 proteins is their ability to bind a multitude of functionally diverse signaling proteins, including kinases, phosphatases, and transmembrane receptors. This plethora of interacting proteins allows 14-3-3 to play important roles in a wide range of vital regulatory processes, such as mitogenic signal transduction, apoptotic cell death, and cell cycle control. In this review, we examine the structural basis for 14-3-3-ligand interactions, proposed functions of 14-3-3 in various signaling pathways, and emerging views of mechanisms that regulate 14-3-3 actions.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Pathogens
                Journal ID (iso-abbrev): Pathogens
                Journal ID (publisher-id): pathogens
                Title: Pathogens
                Publisher: MDPI
                ISSN (Electronic): 2076-0817
                Publication date (Electronic): 27 October 2017
                Publication date Collection: December 2017
                Volume: 6
                Issue: 4
                Electronic Location Identifier: 55
                Affiliations
                [1 ]Department of Microbiology, Instituto Aggeu Magalhães, Fiocruz, Recife 50740-465, PE, Brazil; freireer@ 123456hotmail.com
                [2 ]Department of Microbiology, Immunology & Molecular Genetics, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA 90095, USA; nsturm.ucla@ 123456gmail.com (N.R.S.); dc@ 123456ucla.edu (D.A.C.)
                Author notes
                [* ]Correspondence: opmn@ 123456cpqam.fiocruz.br ; Tel.: +55-81-2101-2500
                Article
                Publisher ID: pathogens-06-00055
                DOI: 10.3390/pathogens6040055
                PMC ID: 5750579
                PubMed ID: 29077018
                SO-VID: 4e9c7f4b-e293-42aa-8a25-94bacd45b409
                Copyright © © 2017 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 20 September 2017
                Date accepted : 22 October 2017
                Categories
                Subject: Review

                Keywords: kinetoplastids,eif4e,translation initiation
                Data availability:
                Keywords: kinetoplastids, eif4e, translation initiation

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