Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

BAG5, a co-chaperone protein, regulates the assembly of HTCA in sperm

ABSTRACT: Acephalic spermatozoa syndrome is severe teratozoospermia, displaying the separation of the sperm head and tail. In 2015, we first reported that genetic ablation of SPATA6 results in the separation of sperm head and tail. Here, we focus on a co-chaperone protein BAG5 that interacts with SPATA6 and expresses in steps 9-16 spermatids. The deficiency of BAG5 in male mice causes the abnormal assembly of the head-tail coupling apparatus (HTCA), leading to acephalic spermatozoa and male infertility. In vivo and in vitro experiments demonstrated that HTCA formation-related proteins (SPATA6), cargo transport-related myosin proteins (MYO5A and MYL6) and dynein proteins (DYNLT1, DCTN1 and DNAL1) were misfolded after loss of BAG5. Further, BAG5 interacts with HSPA8 to regulate its affinity with SPATA6, myosin proteins and dynein proteins. Therefore, we speculate that BAG5 regulates the assembly of the head-tail coupling apparatus (HTCA) by activating the protein-folding function of HSPA8.

INSTRUMENT(S): LTQ

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Testis, Sperm

DISEASE(S): Mixed Disorder As Reaction To Stress

SUBMITTER: 世明甘

LAB HEAD: Shiming Gan

PROVIDER: PXD042965 | Pride | 2023-11-14

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Igg.raw	Raw
	Igg.txt	Txt
	KO1.raw	Raw
	KO2.raw	Raw
	S6.raw	Raw

Items per page:

1 - 5 of 31

Similar Datasets

SUN5 interacts with nuclear membrane LaminB1 and cytoskeletal GTPase Septin12 mediating the sperm head-and-tail junction

Project description:Acephalic spermatozoa syndrome (ASS) is a severe teratospermia with decaudated, decapitated and malformed sperm, resulting in male infertility. Nuclear envelop (NE) protein SUN5 localizes to the junction between the sperm head and tail. Mutations in SUN5 gene have been identified most frequently (33-47%) in ASS cases, and the molecular mechanism needs to be explored. In the present study, we generated Sun5 knockout mice, which presented the phenotype of ASS. Nuclear membrane protein LaminB1, cytoskeletal GTPases Septin12 and Septin2 were identified as potential partners for interacting with SUN5 in mouse testis by immunoprecipitation-mass spectrometry (IP-MS). Further studies demonstrated that SUN5 co-operated with LaminB1, and connected proximal centriole by interacting with Septin12. The binding between SUN5 and Septin12 promoted the aggregation of SUN5 and Septin12 in the sperm neck. The disruption of LaminB1/SUN5/Septin12 complex by Sun5 deficiency caused separation of the Septin12- proximal centriole from the nucleus, leading to the breakage of the head-to-tail junction. Collectively, these data provide new insights into the pathogenesis of ASS caused by SUN5 deficiency.

2024-04-08 | PXD051278 |

In-depth proteomic analysis of carp (Cyprinus carpio L) spermatozoa

Project description:Using a combination of protein fractionation by one-dimensional gel electrophoresis and high performance liquid chromatography - electrospray ionization tandem mass spectrometry, we identified 348 proteins in carp spermatozoa, most of which were for the first time identified in fish. Dynein, tubulin, HSP90, HSP70, HSP60, adenosylhomocysteinase, NKEF-B, brain type creatine kinase, mitochondrial ATP synthase, and valosin containing enzyme represent high abundance proteins in carp spermatozoa. These proteins are functionally related to sperm motility and energy production as well as the protection of sperm against oxidative injury and stress. Moreover, carp sperm is equipped with functionally diverse proteins involved in signal transduction, transcription, translation, protein turnover and transport. About 15% of carp sperm proteins identified here were also detected in seminal plasma which may be a result of leakage from spermatozoa into seminal plasma, adsorption of seminal plasma proteins on spermatozoa surface, and expression in both spermatozoa and cells secreting seminal plasma proteins. The availability of a catalogue of carp sperm proteins provides substantial advances for an understanding of sperm function and for future development of molecular diagnostic tests of carp sperm quality, the evaluation of which is currently limited to certain parameters such as sperm count, morphology and motility or viability.

2014-10-13 | PXD000877 | Pride

HEATR5B associates with dynein-dynactin and selectively promotes motility of AP1- bound endosomal membranes_BioMass@LMB

Project description:The dynein motor complex mediates polarised trafficking of a wide variety of organelles, intracellular vesicles and macromolecules. These functions are dependent on the dynactin 5 complex, which helps recruit cargoes to dynein’s tail region and activates motor movement. How dynein and dynactin orchestrate trafficking of diverse cargoes is unclear. Here, we identify HEATR5B, an interactor of the AP1 clathrin adaptor complex, as a novel player in dynein-dynactin function. HEATR5B is one of several proteins recovered in a biochemical screen for proteins whose association with the human dynein tail complex is augmented by 10 dynactin. We show that HEATR5B binds directly to the dynein tail and dynactin and stimulates motility of AP1-associated endosomal membranes in human cells. We also demonstrate that the HEATR5B homologue in Drosophila is an essential gene that promotes dynein-based transport of AP1-bound membranes to the Golgi apparatus. As HEATR5B lacks the coiledcoil architecture typical of dynein adaptors, our data point to a non-canonical process 15 orchestrating motor function on a specific cargo. We additionally show that HEATR5B promotes association of AP1 with endosomal membranes in a dynein-independent manner. Thus, HEATR5B co-ordinates multiple events in AP1-based trafficking.

2023-10-20 | PXD043387 | Pride

GIV/Girdin Regulates Spatiotemporal Signaling during Sperm Capacitation and is Required for Male Fertility

Project description:For a sperm to successfully fertilize an egg, it must first undergo capacitation in the female reproductive tract, and later undergo acrosomal reaction (AR) upon encountering an egg. How premature AR is avoided despite rapid surges in signaling cascades during capacitation remains unknown. Using a combination of KO mice and cell-penetrating peptides, here we show that GIV (CCDC88A), a guanine nucleotide-exchange factor (GEM) for trimeric GTPases, is highly expressed in spermatocytes and is required for male fertility. GIV is rapidly phosphoregulated on key tyrosine and serine residues in human and murine sperms. These phosphomodifications enable GIV-GEM to orchestrate two distinct compartmentalized signaling programs in the sperm tail and head; in the tail, GIV enhances PI3K→Akt signals, sperm motility and survival, whereas in the head it inhibits cAMP surge and premature AR. Furthermore, GIV transcripts are downregulated in the testes and semen of infertile men. These findings exemplify the spatiotemporally segregated signaling programs that support sperm capacitation and the etiology of infertility in men.

2021-08-16 | GSE171704 | GEO

CTCF contributes in a critical way to spermatogenesis and male fertility

Project description:The CCCTC-binding factor (CTCF) is an architectural protein that governs chromatin organization and gene expression in somatic cells. Here, we show that CTCF regulates chromatin compaction necessary for packaging of the paternal genome into mature sperm. Inactivation of Ctcf in male germ cells in mice (Ctcf-cKO mice) resulted in impaired spermiogenesis and infertility. Residual spermatozoa in Ctcf-cKO mice displayed abnormal head morphology, aberrant chromatin compaction, impaired protamine 1 incorporation into chromatin and accelerated histone depletion. Thus, CTCF regulates chromatin organization during spermiogenesis, contributing to the functional organization of mature sperm.

2016-06-03 | GSE76439 | GEO

Connection of core and and tail Mediator modules restrains transcription from TFIID-dependent promoters [nsRNA-seq]

Project description:The Mediator coactivator complex is divided into four modules: head, middle, tail, and kinase. Deletion of the architectural subunit Med16 separates core Mediator (cMed), comprising the head, middle, and scaffold (Med14), from the tail. However, the direct global effects of tail/cMed disconnection are unclear. We find that rapid depletion of Med16 downregulates genes that require the SAGA complex for full expression, consistent with their reported tail dependence, but also moderately overactivates TFIID-dependent genes in a manner partly dependent on the separated tail, which remains associated with upstream activating sequences. Suppression of TBP dynamics via removal of the Mot1 ATPase partially restores normal transcriptional activity to Med16-depleted cells, suggesting that cMed/tail separation results in an imbalance in the levels PIC formation at SAGA-requiring and TFIID-dependent genes. We suggest that the preferential regulation of SAGA-requiring genes by tailed Mediator helps maintain a proper balance of transcription between these genes and those more dependent on TFIID.

2021-07-30 | GSE169747 | GEO

Connection of core and and tail Mediator modules restrains transcription from TFIID-dependent promoters [ChEC-seq]

2021-07-30 | GSE169746 | GEO

Connection of core and and tail Mediator modules restrains transcription from TFIID-dependent promoters [ChEC-seq Med16-AID]

2021-07-30 | GSE179765 | GEO

Connection of core and tail Mediator modules restrains transcription from TFIID-dependent promoters [ChIP-Seq]

Project description:The Mediator coactivator complex is divided into four modules: head, middle, tail, and kinase. Deletion of the architectural subunit Med16 separates core Mediator (cMed), comprising the head, middle, and scaffold (Med14), from the tail. However, the direct global effects of tail/cMed disconnection are unclear. We find that rapid depletion of Med16 downregulates genes that require the SAGA complex for full expression, consistent with their reported tail dependence, but also moderately overactivates TFIID-dependent genes in a manner partly dependent on the separated tail, which remains associated with upstream activating sequences. Suppression of TBP dynamics via removal of the Mot1 ATPase partially restores normal transcriptional activity to Med16-depleted cells, suggesting that cMed/tail separation results in an imbalance in the levels of PIC formation at SAGA-requiring and TFIID-dependent genes. We suggest that the preferential regulation of SAGA-requiring genes by tailed Mediator helps maintain a proper balance of transcription between these genes and those more dependent on TFIID.

2021-07-30 | GSE171981 | GEO

Sperm heterogeneity and DNMT/TET activities do not account for sperm DNA methylation changes observed in the epididymis

Project description:Following their production in the testis, spermatozoa enter the epididymis to gain their motility and fertilizing abilities. This post-testicular maturation coincides with sperm epigenetic profile changes that influence the progeny outcome. While recent studies underscored the dynamics of small non-coding RNAs in the maturing spermatozoa, little is known regarding sperm methylation changes and their impact at the post-fertilization level. To map out the sperm methylome dynamics, we purified spermatozoa by FACS from the testis and the different epididymal segments (i.e. caput, corpus and cauda) of CAG/su9-DsRed2; Acr3-EGFP transgenic mice. Reduced-Representation Bisulfite Sequencing (RRBS-Seq) performed on DNA from these respective sperm populations indicated that high methylation changes were observed between spermatozoa from the caput vs. testis with 5546 entries meeting our threshold values (q value < 0.01, methylation difference above 25 %). Most of these changes were transitory during epididymal sperm maturation according to the low number of entries identified between spermatozoa from cauda vs. testis.

2022-03-10 | GSE191051 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data