Expression, sorting, and segregation of Golgi proteins during germ cell differentiation in the testis
| Autor: | Kewei Ma, Paul H. G. Simon, John J.M. Bergeron, Jeffrey Smirle, Elliot Byrne, Pamela H. Cameron, Charles E. Smith, Julia Fernandez-Rodriguez, Ali Fazel, Tommy Nilsson, Louis Hermo, Robert E. Kearney, Hojatollah Vali, Catherine E. Au |
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| Rok vydání: | 2015 |
| Předmět: |
Big Data
Male endocrine system Cellular differentiation Golgi Apparatus Biology Endoplasmic Reticulum Rats Sprague-Dawley symbols.namesake Cell Movement Testis medicine Animals Humans Spermatogenesis Acrosome Molecular Biology Secretory pathway Membrane Glycoproteins Endoplasmic reticulum Membrane Proteins Cell Differentiation Hep G2 Cells Cell Biology Golgi apparatus Spermatids Spermatozoa Rats Cell biology Protein Transport medicine.anatomical_structure Membrane protein Cytoplasm symbols Germ cell |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e14-12-1632 |
| Popis: | A total of 1318 proteins characterized in the male germ cell Golgi apparatus reveal a new germ cell–specific Golgi marker and a new pan-Golgi marker for all cells. The localization of these and other Golgi proteins reveals differential expression linked to mitosis, meiosis, acrosome formation, and postacrosome Golgi migration and destination in the late spermatid. The molecular basis of changes in structure, cellular location, and function of the Golgi apparatus during male germ cell differentiation is unknown. To deduce cognate Golgi proteins, we isolated germ cell Golgi fractions, and 1318 proteins were characterized, with 20 localized in situ. The most abundant protein, GL54D of unknown function, is characterized as a germ cell–specific Golgi-localized type II integral membrane glycoprotein. TM9SF3, also of unknown function, was revealed to be a universal Golgi marker for both somatic and germ cells. During acrosome formation, several Golgi proteins (GBF1, GPP34, GRASP55) localize to both the acrosome and Golgi, while GL54D, TM9SF3, and the Golgi trafficking protein TMED7/p27 are segregated from the acrosome. After acrosome formation, GL54D, TM9SF3, TMED4/p25, and TMED7/p27 continue to mark Golgi identity as it migrates away from the acrosome, while the others (GBF1, GPP34, GRASP55) remain in the acrosome and are progressively lost in later steps of differentiation. Cytoplasmic HSP70.2 and the endoplasmic reticulum luminal protein-folding enzyme PDILT are also Golgi recruited but only during acrosome formation. This resource identifies abundant Golgi proteins that are expressed differentially during mitosis, meiosis, and postacrosome Golgi migration, including the last step of differentiation. |
| Databáze: | OpenAIRE |
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