Page 44 - GPD-2-2
P. 44

Gene & Protein in Disease                                                  MPDZ regulates sperm motility



            28.  Tetzlaff F, Adam MG, Feldner A, et al., 2018, MPDZ promotes   2018, Role of the Crumbs proteins in ciliogenesis, cell
               DLL4-induced Notch signaling during angiogenesis.   migration and actin organization.  Semin Cell Dev Biol,
               Elife, 7: e32860.                                  81: 13–20.
               https://doi.org/10.7554/eLife.32860                https://doi.org/10.1016/j.semcdb.2017.10.018
            29.  Liu W, Huang Y, Wang D, et al., 2021, MPDZ as a novel   40.  Thiery JP, Acloque H, Huang RY,  et al., 2009, Epithelial-
               epigenetic silenced tumor suppressor inhibits growth and   mesenchymal transitions in development and disease. Cell,
               progression of lung cancer through the Hippo-YAP pathway.   139: 871–890.
               Oncogene, 40: 4468–4485.
                                                                  https://doi.org/10.1016/j.cell.2009.11.007
               https://doi.org/10.1038/s41388-021-01857-8
                                                               41.  Zitranski N, Borth H, Ackermann F,  et al., 2010, The
            30.  Ackermann F, Zitranski N, Heydecke D,  et al., 2008, The   “acrosomal synapse”: Subcellular organization by lipid
               Multi-PDZ domain protein MUPP1 as a lipid raft-associated   rafts and scaffolding proteins exhibits high similarities in
               scaffolding protein controlling the acrosome reaction in   neurons and mammalian spermatozoa. Commun Integr Biol,
               mammalian spermatozoa. J Cell Physiol, 214: 757–768.   3: 513–521.
               https://doi.org/10.1002/jcp.21272                  https://doi.org/10.4161/cib.3.6.13137
            31.  Lu L, Zhu F, Zhang M,  et al., 2018, Gene regulation and   42.  Ackermann  F,  Zitranski  N,  Borth  H,  et al.,  2009,
               suppression of Type  I interferon signaling by STAT3 in   CaMKIIalpha interacts with multi-PDZ domain protein
               diffuse large B cell lymphoma. Proc Natl Acad Sci U S A, 115:   MUPP1 in spermatozoa and prevents spontaneous
               E498–E505.                                         acrosomal exocytosis. J Cell Sci, 122: 4547–4557.
               https://doi.org/10.1073/pnas.1715118115            https://doi.org/10.1242/jcs.058263
            32.  Dong X, He Y, Ye F, et al., 2021, Vitamin D3 ameliorates   43.  Heydecke D, Meyer D, Ackermann F, et al., 2006, The multi
               nitrogen mustard-induced cutaneous inflammation by   PDZ domain protein MUPP1 as a putative scaffolding
               inactivating the NLRP3 inflammasome through the SIRT3-  protein for organizing signaling complexes in the acrosome
               SOD2-mtROS signaling pathway. Clin Transl Med, 11: e312.   of mammalian spermatozoa. J Androl, 27: 390–404.
               https://doi.org/10.1002/ctm2.312                   https://doi.org/10.2164/jandrol.05166
            33.  WHO, 2010, WHO Laboratory Manual for the      44.  Aravindan  RG, Fomin  VP, Naik  UP,  et al., 2012,  CASK
                                                      th
               Examination and Processing of Human Semen. 5   ed.   interacts with PMCA4b and JAM-A on the mouse sperm
               Geneva: WHO Press.                                 flagellum to regulate Ca2+ homeostasis and motility. J Cell
            34.  Becamel C,  Figge A, Poliak S,  et  al., 2001, Interaction of   Physiol, 227: 3138–3150.
               serotonin 5-hydroxytryptamine Type  2C receptors with      https://doi.org/10.1002/jcp.24000
               PDZ10  of  the  multi-PDZ  domain protein  MUPP1.  J  Biol
               Chem, 276: 12974–12982.                         45.  Burkin HR, Zhao L, Miller DJ, 2004, CASK is in the
                                                                  mammalian sperm head and is processed during epididymal
               https://doi.org/10.1074/jbc.M008089200             maturation. Mol Reprod Dev, 68: 500–506.
            35.  Tramontano A, 2017, The computational prediction of      https://doi.org/10.1002/mrd.20108
               protein assemblies. Curr Opin Struct Biol, 46: 170–175.
                                                               46.  Wang H, McGoldrick LL, Chung JJ, 2021, Sperm ion
               https://doi.org/10.1016/j.sbi.2017.10.006          channels and transporters in male fertility and infertility.
            36.  Meseguer A, Bota P, Fernández-Fuentes N,  et  al.,   Nat Rev Urol, 18: 46–66.
               2022, Prediction of protein-protein binding affinities      https://doi.org/10.1038/s41585-020-00390-9
               from unbound protein structures.  Methods Mol Biol,
               2385: 335–351.                                  47.  Li HG, Ding XF, Liao AH,  et  al., 2007, Expression of
                                                                  CatSper family transcripts in the mouse testis during post-
               https://doi.org/10.1007/978-1-0716-1767-0_16       natal development and human ejaculated spermatozoa:
            37.  Yueh C, Hall DR, Xia B, et al., 2017, ClusPro-DC: Dimer   Relationship to sperm motility.  Mol Hum Reprod,
               classification by the cluspro server for protein-protein   13: 299–306.
               docking. J Mol Biol, 429: 372–381.                 https://doi.org/10.1093/molehr/gam009
               https://doi.org/10.1016/j.jmb.2016.10.019       48.  Verma P, Parte P, 2021, Revisiting the characteristics of
            38.  Kozakov D, Hall DR, Xia B, et al., 2017, The ClusPro web   testicular germ cell lines GC-1(spg) and GC-2(spd)ts. Mol
               server for protein-protein docking. Nat Protoc, 12: 255–278.   Biotechnol, 63: 941–952.
               https://doi.org/10.1038/nprot.2016.169             https://doi.org/10.1007/s12033-021-00352-5
            39.  Bazellières E, Aksenova V, Barthélémy-Requin M,  et al.,   49.  Mata-Rocha M, Hernández-Sánchez J, Guarneros G, et al.,


            Volume 2 Issue 2 (2023)                         11                        https://doi.org/10.36922/gpd.397
   39   40   41   42   43   44   45   46   47   48   49