<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lazzari, Elisa</style></author><author><style face="normal" font="default" size="100%">Meroni, Germana</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">TRIM32 ubiquitin E3 ligase, one enzyme for several pathologies: From muscular dystrophy to tumours.</style></title><secondary-title><style face="normal" font="default" size="100%">Int J Biochem Cell Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Int. J. Biochem. Cell Biol.</style></alt-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2016 Jul 22</style></date></pub-dates></dates><language><style face="normal" font="default" size="100%">ENG</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;TRIM32 is a member of the TRIpartite Motif family characterised by the presence of an N-terminal three-domain-module that includes a RING domain, which confers E3 ubiquitin ligase activity, one or two B-box domains and a Coiled-Coil region that mediates oligomerisation. Several TRIM32 substrates were identified including muscular proteins and proteins involved in cell cycle regulation and cell motility. As ubiquitination is a versatile post-translational modification that can affect target turnover, sub-cellular localisation or activity, it is likely that diverse substrates may be differentially affected by TRIM32-mediated ubiquitination, reflecting its multi-faceted roles in muscle physiology, cancer and immunity. With particular relevance for muscle physiology, mutations in TRIM32 are associated with autosomal recessive Limb-Girdle Muscular Dystrophy 2H, a muscle-wasting disease with variable clinical spectrum ranging from almost asymptomatic to wheelchair-bound patients. In this review, we will focus on the ability of TRIM32 to mark specific substrates for proteasomal degradation discussing how the TRIM32-proteasome axis may (i) be important for muscle homeostasis and for the pathogenesis of muscular dystrophy; and (ii) define either an oncogenic or tumour suppressive role for TRIM32 in the context of different types of cancer.&lt;/p&gt;</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/27458054?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Boding, Lasse</style></author><author><style face="normal" font="default" size="100%">Hansen, Ann K</style></author><author><style face="normal" font="default" size="100%">Meroni, Germana</style></author><author><style face="normal" font="default" size="100%">Levring, Trine B</style></author><author><style face="normal" font="default" size="100%">Woetmann, Anders</style></author><author><style face="normal" font="default" size="100%">Ødum, Niels</style></author><author><style face="normal" font="default" size="100%">Bonefeld, Charlotte M</style></author><author><style face="normal" font="default" size="100%">Geisler, Carsten</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">MID2 can substitute for MID1 and control exocytosis of lytic granules in cytotoxic T cells.</style></title><secondary-title><style face="normal" font="default" size="100%">APMIS</style></secondary-title><alt-title><style face="normal" font="default" size="100%">APMIS</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytoplasmic Granules</style></keyword><keyword><style  face="normal" font="default" size="100%">Exocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Interferon-gamma</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Inbred C57BL</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword><keyword><style  face="normal" font="default" size="100%">Microtubule-Associated Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">T-Lymphocytes, Cytotoxic</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Up-Regulation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2015 Aug</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">123</style></volume><pages><style face="normal" font="default" size="100%">682-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We have recently shown that the E3 ubiquitin ligase midline 1 (MID1) is upregulated in murine cytotoxic lymphocytes (CTL), where it controls exocytosis of lytic granules and the killing capacity. Accordingly, CTL from MID1 knock-out (MID1(-/-)) mice have a 25-30% reduction in exocytosis of lytic granules and cytotoxicity compared to CTL from wild-type (WT) mice. We wondered why the MID1 gene knock-out did not affect exocytosis and cytotoxicity more severely and speculated whether MID2, a close homologue of MID1, might partially compensate for the loss of MID1 in MID1(-/-) CTL. Here, we showed that MID2, like MID1, is upregulated in activated murine T cells. Furthermore, MID1(-/-) CTL upregulated MID2 two-twenty-fold stronger than CTL from WT mice, suggesting that MID2 might compensate for MID1. In agreement, transfection of MID2 into MID1(-/-) CTL completely rescued exocytosis of lytic granules in MID1(-/-) CTL, and vice versa, knock-down of MID2 inhibited exocytosis of lytic granules in both WT and MID1(-/-) CTL, demonstrating that both MID1 and MID2 play a central role in the regulation of granule exocytosis and that functional redundancy exists between MID1 and MID2 in CTL.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25924778?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Boding, Lasse</style></author><author><style face="normal" font="default" size="100%">Hansen, Ann K</style></author><author><style face="normal" font="default" size="100%">Meroni, Germana</style></author><author><style face="normal" font="default" size="100%">Johansen, Bo B</style></author><author><style face="normal" font="default" size="100%">Braunstein, Thomas H</style></author><author><style face="normal" font="default" size="100%">Bonefeld, Charlotte M</style></author><author><style face="normal" font="default" size="100%">Kongsbak, Martin</style></author><author><style face="normal" font="default" size="100%">Jensen, Benjamin A H</style></author><author><style face="normal" font="default" size="100%">Woetmann, Anders</style></author><author><style face="normal" font="default" size="100%">Thomsen, Allan R</style></author><author><style face="normal" font="default" size="100%">Odum, Niels</style></author><author><style face="normal" font="default" size="100%">von Essen, Marina R</style></author><author><style face="normal" font="default" size="100%">Geisler, Carsten</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Midline 1 directs lytic granule exocytosis and cytotoxicity of mouse killer T cells.</style></title><secondary-title><style face="normal" font="default" size="100%">Eur J Immunol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Eur. J. Immunol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytotoxicity, Immunologic</style></keyword><keyword><style  face="normal" font="default" size="100%">Exocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Flow Cytometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Transgenic</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Reverse Transcriptase Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Secretory Vesicles</style></keyword><keyword><style  face="normal" font="default" size="100%">T-Lymphocytes, Cytotoxic</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2014 Oct</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">44</style></volume><pages><style face="normal" font="default" size="100%">3109-18</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Midline 1 (MID1) is a microtubule-associated ubiquitin ligase that regulates protein phosphatase 2A activity. Loss-of-function mutations in MID1 lead to the X-linked Opitz G/BBB syndrome characterized by defective midline development during embryogenesis. Here, we show that MID1 is strongly upregulated in murine cytotoxic lymphocytes (CTLs), and that it controls TCR signaling, centrosome trafficking, and exocytosis of lytic granules. In accordance, we find that the killing capacity of MID1(-/-) CTLs is impaired. Transfection of MID1 into MID1(-/-) CTLs completely rescued lytic granule exocytosis, and vice versa, knockdown of MID1 inhibited exocytosis of lytic granules in WT CTLs, cementing a central role for MID1 in the regulation of granule exocytosis. Thus, MID1 orchestrates multiple events in CTL responses, adding a novel level of regulation to CTL activation and cytotoxicity.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25043946?dopt=Abstract</style></custom1></record></records></xml>