Expression, sorting, and segregation of Golgi proteins during germ cell differentiation in the testis

Au, Catherine; Hermo, Louis; Byrne, Elliot; Smirle, Jeffrey; Fazel, Ali; Simon, Paul; Kearney, Robert E.; Cameron, Pamela H.; Smith, Charles E.; Vali, Hojatollah; Fernández-Rodrı́guez, Julia; Ma, Kewei; Nilsson, Tommy; Bergeron, John J.M.

doi:10.1091/mbc.e14-12-1632

Cited by 25 publications

(53 citation statements)

References 91 publications

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“…Acrosome development occurs during early spermiogenesis and results from the assembly of pro-acrosomic vesicles. These vesicles originate from the Golgi apparatus and GRASP55 has been reported to be specifically associated to the Golgi apparatus and acrosome of step 1–7 rat spermatids, which suggests that this protein plays a specific function in acrosome development [45]. Our results confirmed this hypothesis and demonstrated that this function relies, at least partially, on the transient interaction between GRASP55 and JAM-C during early spermiogenesis in mice (step 1–7 spermatids).…”

Section: Discussionsupporting

confidence: 84%

Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis

et al. 2017

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Spermatogenesis is a dynamic process that is regulated by adhesive interactions between germ and Sertoli cells. Germ cells express the Junctional Adhesion Molecule-C (JAM-C, encoded by Jam3), which localizes to germ/Sertoli cell contacts. JAM-C is involved in germ cell polarity and acrosome formation. Using a proteomic approach, we demonstrated that JAM-C interacted with the Golgi reassembly stacking protein of 55 kDa (GRASP55, encoded by Gorasp2) in developing germ cells. Generation and study of Gorasp2-/- mice revealed that knock-out mice suffered from spermatogenesis defects. Acrosome formation and polarized localization of JAM-C in spermatids were altered in Gorasp2-/- mice. In addition, Golgi morphology of spermatocytes was disturbed in Gorasp2-/- mice. Crystal structures of GRASP55 in complex with JAM-C or JAM-B revealed that GRASP55 interacted via PDZ-mediated interactions with JAMs and induced a conformational change in GRASP55 with respect of its free conformation. An in silico pharmacophore approach identified a chemical compound called Graspin that inhibited PDZ-mediated interactions of GRASP55 with JAMs. Treatment of mice with Graspin hampered the polarized localization of JAM-C in spermatids, induced the premature release of spermatids and affected the Golgi morphology of meiotic spermatocytes.

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Section: Discussionsupporting

confidence: 84%

Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis

et al. 2017

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“…In this way, we could compare if the protein composition of the Golgi cisternae of the HB was comparable to that of germ cells of the testis. Protein abundances were estimated from spectral counting (redundant peptides) with a comparison of the proteins characterized in each of the n = 3 separate isolates of both the testis Golgi fractions with those of HB isolated from epididymal spermatozoa (Au et al ., ,b). Proteins were subdivided into 22 functional categories as described by Gilchrist et al .…”

Section: Isolation and Characterization Of The Protein Makeup Of The mentioning

confidence: 99%

“…In order to determine a functional role for the HB of spermatozoa, subcellular fractions of isolated HBs from adult rat caput epididymal spermatozoa were characterized by quantitative tandem mass spectrometry (Au et al ., 2015a). Concomitantly, the spherical compact Golgi apparatus characteristic of germ cells was isolated from whole testis homogenates (Au et al ., 2015b). In this way, we could compare if the protein composition of the Golgi cisternae of the HB was comparable to that of germ cells of the testis.…”

Section: Isolation and Characterization Of The Protein Makeup Of The mentioning

confidence: 99%

“…Remarkably, spermatozoa acquire their maturational features, that is, motility and fertility as they pass through the epididymis (Orgebin‐Crist, ; Robaire & Hermo, ; Robaire & Hinton, ), an event coincident with the presence of the droplet on spermatozoa (Hermo et al ., , ; Cooper, ; Gervasi & Visconti, ), suggesting a cause–effect relationship. In this review, we highlight our data on the protein composition of organelles of the droplet to define their functional roles in relation to sperm maturation (Au et al ., ,b; Hermo et al ., ).…”

Section: Introduction: Background On the Formation And Constituents Omentioning

confidence: 98%

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Dark side of the epididymis: tails of sperm maturation

et al. 2019

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Background: The Hermes body (HB) previously called the cytoplasmic droplet is a focal distension of the flagellar cytoplasm of epididymal spermatozoa consisting mainly of isolated flattened Golgi cisternae. Objective: To define a functional role for the HB of epididymal spermatozoa. Methods: Isolated fractions of HBs of epididymal spermatozoa were prepared and by quantitative tandem mass spectrometry revealed 1511 proteins. Results: The glucose transporter GLUT-3 was the most abundant protein followed by hexokinase 1, which along with the presence of all glycolytic enzymes suggested a role for the HB in glycolysis. Several TMED/p24 Golgi trafficking proteins were abundant with TMED7/p27 and TMED2/p24 defining the identity of the flattened cisternae within the HB as Golgi, along with the known Golgi proteins, GBF1, GOLPH3, Man2a1, and ManIIX. The Golgi trafficking protein TMED7/p27 via small 50-nm vesicles emanating from the Golgi cisternae was proposed to transport GLUT-3 to the plasma membrane for ATP production related to sperm motility. The internal membranes revealed abundant proteins not only of Golgi cisternae, but also of endoplasmic reticulum and endosomes. COPI and COPII coats, clathrin, SNAREs, annexins, atlastins, and GTPases were identified for vesicular trafficking and membrane fusion, in addition to ribosomes, stress proteins for protection, proteasome proteins involved in degradation, and cytoskeletal elements for migration of the HB along the flagellum. The biogenesis of the HB occurring at step 19 spermatids of the testis just prior to their release was uncovered as a key step in germ cell differentiation, where several proteins were expressed, some for the first time. Conclusion: As epididymal spermatozoa undergo remodeling of their protein makeup through selective degradation of sperm proteins during epididymal transit, then remodeling as a consequence of new protein synthesis is not excluded by our observations.

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“…There are close to 500 glycogenes encoded in the human genome , whose expression is regulated at multiple levels: transcription, regulation of transcript and/or protein half‐life. Several studies have demonstrated a change in expression of glycogenes in response to cell intrinsic or extrinsic factors . For instance, epigenetic mechanisms have been shown to regulate the changes in glycogene expression that leads to a switch from neutral globo and lacto series GSLs to acidic ganglio‐series GSLs during neuronal differentiation .…”

Section: Factors Affecting Glycan Outputmentioning

confidence: 99%

Translation of genome to glycome: role of the Golgi apparatus

et al. 2019

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Glycans are one of the four biopolymers of the cell and they play important roles in cellular and organismal physiology. They consist of both linear and branched structures and are synthesized in a nontemplated manner in the secretory pathway of mammalian cells with the Golgi apparatus playing a key role in the process. In spite of the absence of a template, the glycans synthesized by a cell are not a random collection of possible glycan structures but a distribution of specific glycans in defined quantities that is unique to each cell type (Cell type here refers to distinct cell forms present in an organism that can be distinguished based on morphological, phenotypic and/or molecular criteria.) While information to produce cell type‐specific glycans is encoded in the genome, how this information is translated into cell type‐specific glycome (Glycome refers to the quantitative distribution of all glycan structures present in a given cell type.) is not completely understood. We summarize here the factors that are known to influence the fidelity of glycan biosynthesis and integrate them into known glycosylation pathways so as to rationalize the translation of genetic information to cell type‐specific glycome.

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Expression, sorting, and segregation of Golgi proteins during germ cell differentiation in the testis

Cited by 25 publications

References 91 publications

Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis

Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis

Dark side of the epididymis: tails of sperm maturation

Translation of genome to glycome: role of the Golgi apparatus

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