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      Ttc7a regulates hematopoietic stem cell functions while controlling the stress-induced response

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          Abstract

          The molecular machinery that regulates the balance between self-renewal and differentiation properties of hematopoietic stem cells (HSC) has yet to be characterized in detail. Here we found that the tetratricopeptide repeat domain 7 A (Ttc7a) protein, a putative scaffold protein expressed by HSC, acts as an intrinsic regulator of the proliferative response and the self-renewal potential of murine HSC in vivo. Loss of Ttc7a consistently enhanced the competitive repopulating ability of HSC and their intrinsic capacity to replenish the hematopoietic system after serial cell transplantations, relative to wildtype cells. Ttc7a-deficient HSC exhibit a different transcriptomic profile for a set of genes controlling the cellular response to stress, which was associated with increased proliferation in response to chemically induced stress in vitro and myeloablative stress in vivo. Our results therefore revealed a previously unrecognized role of Ttc7a as a critical regulator of HSC stemness. This role is related, at least in part, to regulation of the endoplasmic reticulum stress response.

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          TPR proteins: the versatile helix.

          Luca D'Andrea, Lynne Regan (2003)
          Tetratrico peptide repeat (TPR) proteins have several interesting properties, including their folding characteristics, modular architecture and range of binding specificities. In the past five years, many 3D structures of TPR domains have been solved, revealing at a molecular level the versatility of this basic fold. Here, we discuss the structure of TPRs and highlight the diversity of arrangements and functions that are associated with these ubiquitous domains. Genomic analyses of the distribution of TPR domains are presented along with implications for protein engineering.
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            Regulation of the HIF-1alpha level is essential for hematopoietic stem cells.

            Keiyo Takubo, Nobuhito Goda, Wakako Yamada … (2010)
            Hematopoietic stem cells (HSCs) are sustained in a specific microenvironment known as the stem cell niche. Mammalian HSCs are kept quiescent in the endosteal niche, a hypoxic zone of the bone marrow (BM). In this study, we show that normal HSCs maintain intracellular hypoxia and stabilize hypoxia-inducible factor-1alpha (HIF-1alpha) protein. In HIF-1alpha-deficient mice, the HSCs lost their cell cycle quiescence and HSC numbers decreased during various stress settings including bone marrow transplantation, myelosuppression, or aging, in a p16(Ink4a)/p19(Arf)-dependent manner. Overstabilization of HIF-1alpha by biallelic loss of an E3 ubiquitin ligase for HIF-1alpha (VHL) induced cell cycle quiescence in HSCs and their progenitors but resulted in an impairment in transplantation capacity. In contrast, monoallelic loss of VHL induced cell cycle quiescence and improved BM engraftment during bone marrow transplantation. These data indicate that HSCs maintain cell cycle quiescence through the precise regulation of HIF-1alpha levels. Copyright 2010 Elsevier Inc. All rights reserved.
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              Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.

              C Scheufler, A Brinker, G Bourenkov … (2000)
              The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both sequences end with the motif EEVD. The crystal structures of the TPR-peptide complexes show the peptides in an extended conformation, spanning a groove in the TPR domains. Peptide binding is mediated by electrostatic interactions with the EEVD motif, with the C-terminal aspartate acting as a two-carboxylate anchor, and by hydrophobic interactions with residues upstream of EEVD. The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Haematologica
                Journal ID (iso-abbrev): Haematologica
                Journal ID (hwp): haematol
                Journal ID (publisher-id): Haematologica
                Title: Haematologica
                Publisher: Ferrata Storti Foundation
                ISSN (Print): 0390-6078
                ISSN (Electronic): 1592-8721
                Publication date (Print): January 2020
                Publication date (Electronic preprint): 19 April 2019
                Volume: 105
                Issue: 1
                Pages: 59-70
                Affiliations
                [1 ]Laboratory of Normal and Pathological Homeostasis of the Immune System, INSERM UMR 1163, Imagine Institute, Paris
                [2 ]Université Paris Descartes -Sorbonne Paris Cité, Imagine Institute, Paris
                [3 ]Bioinformatic Platform, INSERM UMR 1163, Université Paris Descartes-Sorbonne Paris Cité, Imagine Institute, Paris
                [4 ]Structure Fédérative de Recherche (SFR) Necker, INSERM US24/CNRS UMS 3633, Paris
                [5 ]Assistance Publique-Hôpitaux de Paris, Hôpital Necker-Enfants Malades Immunology and Pediatric Hematology Department, Paris
                [6 ]Collège de France, Paris, France
                [7 ]INSERM UMR1163, Paris
                [8 ]Assistance Publique-Hôpitaux de Paris, Hôpital Necker-Enfants Malades, Centre d’Etudes des Déficits Immunitaires, Paris
                [9 ]Centre National de la Recherche Scientifique – CNRS, Paris, France
                Author notes
                Correspondence: GENEVIÈVE DE SAINT BASILE genevieve.de-saint-basile@ 123456inserm.fr ; FERNANDO E. SEPULVEDA fernando.sepulveda@ 123456inserm.fr
                [*]

                These authors contributed equally to this work

                Article
                Publisher ID: 1050059
                DOI: 10.3324/haematol.2018.207100
                PMC ID: 6939534
                PubMed ID: 31004027
                SO-VID: d4dfe1d2-02ef-4de8-8946-1190c8e19d83
                Copyright © Copyright© 2020 Ferrata Storti Foundation
                License:

                Material published in Haematologica is covered by copyright. All rights are reserved to the Ferrata Storti Foundation. Use of published material is allowed under the following terms and conditions:

                https://creativecommons.org/licenses/by-nc/4.0/legalcode. Copies of published material are allowed for personal or internal use. Sharing published material for non-commercial purposes is subject to the following conditions:

                https://creativecommons.org/licenses/by-nc/4.0/legalcode, sect. 3. Reproducing and sharing published material for commercial purposes is not allowed without permission in writing from the publisher.

                History
                Date received : 18 September 2018
                Date accepted : 17 April 2019
                Categories
                Subject: Article
                Subject: Hematopoiesis

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