Activation of a G Protein Complex by Aggregation of β-1,4-Galactosyltransferase on the Surface of Sperm

Gong, Xianghui; Dubois, Daniel H.; Miller, David J.; Shur, Barry D.

doi:10.1126/science.7569899

Cited by 156 publications

(88 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This idea was supported by reports that the addition of solubilized zona pellucida can induce acrosome reaction [12], and that a partial ZP3 sequence can accomplish the same effect [22]. Based on this context, zona binding proteins were assumed to initiate the signaling cascade leading to acrosome reaction [16] and various zona binding proteins were purified from spermatozoa. However, the gene disruption of these factors did not show a significant phenotype in fertilization as indicated in Table 2.…”

Section: Zona-induced Acrosome Reaction Must Be Reconsideredmentioning

confidence: 69%

Mechanism of Fertilization: A Modern View

Okabe

2014

Exp. Anim.

View full text Add to dashboard Cite

Despite numerous studies on mammalian fertilization, the mechanisms of fertilizationincluding the timing of acrosome reaction-remain largely unknown; more accurately described, the classical theory built upon years of layered experimental data is being challenged by recent conflicting evidence provided by gene-manipulated animals. Although in vitro fertilization remains our central research tool, the classical theory's decline reminds us of the importance of in vivo observations. Here, I describe the essential roles of gene-manipulated animals in elucidating the mechanism of fertilization and the pitfalls of in vitro fertilization studies trapping many researchers.

show abstract

Section: Zona-induced Acrosome Reaction Must Be Reconsideredmentioning

confidence: 69%

Mechanism of Fertilization: A Modern View

Okabe

2014

Exp. Anim.

View full text Add to dashboard Cite

show abstract

“…However, there are several exceptional cases in which single-transmembrane receptors or receptor-like proteins are directly linked to G proteins (Murayama et al 1990;Nishimoto et al 1993;Gong et al 1995;Sun et al 1995Sun et al , 1997. Most importantly, APP has been shown to directly interact with Go, but not Gi, and furthermore to activate Go in a phospholipid vesicle system (Okamoto and Nishimoto 1992;Nishimoto et al 1993;Brouillet et al 1999).…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization of neurohybrid cell death induced by Alzheimer's amyloid‐β peptides via p75NTR/PLAIDD

Hashimoto¹,

Kaneko²,

Tsukamoto³

et al. 2004

Journal of Neurochemistry

View full text Add to dashboard Cite

One of the most important pathological features of Alzheimer's disease (AD) is extracellular senile plaques, whose major component is amyloid-b peptides (Ab). Ab binds to the extracellular domain of p75NTR (p75 neurotrophin receptor) and induces neuronal cell death. We investigated the molecular mechanism of Ab-induced neurotoxicity in detail from the standpoint of interaction between p75NTR and its recently identified relative, PLAIDD (p75-like apoptosis-inducing death domain). Using F11 neuronal hybrid cells, we demonstrate that there are two distinct pathways for Abinduced toxicity mediated by p75NTR. One pathway that has been previously elucidated, is mediated by p75NTR, Go, JNK, NADPH oxidase and caspase3-related caspases. We found that PLAIDD and Gi proteins, heterotrimeric G proteins, are involved in the alternative Ab-induced neurotoxicity mediated by p75NTR. The alternative pathway triggered by Ab is thus mediated by p75NTR, PLAIDD, Gi, JNK, NADPH oxidase and caspase3-related caspases. In addition, we found that HN, ADNF, IGF-I, or bFGF inhibits both pathways of Ab-induced neurotoxicity mediated by p75NTR. Amyloid-b peptides (Ab) are the major constituent of the senile plaques in Alzheimer's disease (AD). Ab, the 39-43 amino acids peptide, is produced by the b-and c-secretasemediated cleavage of amyloid precursor protein (APP). Formation and accumulation of Ab have been inferred to contribute to the development of AD. In vitro, increased levels of Ab concentration cause cell death in primary cultured neurons as well as some neuronal line cells (Yankner et al. 1989;Loo et al. 1993;Gschwind and Huber 1995;Kaneko et al. 1995;Pike et al. 1997;Giovanni et al. 1999;Sudo et al. 2001). However, the precise mechanism underlying Ab neurotoxicity remains to be elucidated.One possible mechanism for Ab-induced neurotoxicity is that Ab binds to its putative receptor on the neuronal cell membrane and triggers the intracellular death signal. Multiple proteins have been so far claimed to be candidates for the Ab receptor. They include the receptors for the endoplasmic reticulum Ab-binding dehydrogenase (ERAB;Yan et al. 1997a), the advanced glycation end products (Yan et al. 1997b), the a7 nicotinic acetylcholine receptor (Wang Address correspondence and reprint requests to M. Matsuoka, Department of Pharmacology, KEIO University School of Medicine, Shinanomachi, Tokyo, Japan. E-mail: sakimatu@sc.itc.keio.ac.jpAbbreviations used: Ab, amyloid beta; AD, Alzheimer's disease; ADNF, activity-dependent neurotrophic factor; APO, apocynin; APP, amyloid precursor protein; BBP-1, b-amyloid binding protein-1; bFGF, basic fibroblast growth factor; DPI, diphenyleneiodonium chloride; ERAB, endoplasmic reticulum Ab-binding dehydogenase; FBS, fetal bovine serum; GEE, gluthione-ethyl-ester; HN, Humanin; HRP, horseradish peroxidase; JNK, c-Jun N-terminal kinase; NFkB, nuclear factorkB; NOS, nitric oxide synthase; (p75-like apoptosis-inducing death domain) p75NTR, 75 kDa neurotrophin receptor; PTX, pertussis toxin; ROS, reactive ox...

show abstract

“…2B). Similarly, membranes from transgenic sperm overexpressing GalT show increased rates of both basal and ZP-dependent G-protein activation, relative to wild-type sperm, and transgenic sperm show greatly accelerated rates of acrosomal exocytosis (Gong et al, 1995). Thus, increasing GalT expression on sperm makes them hypersensitive to their ZP3 ligand.…”

Section: Evidence Implicating Sperm Galt As An Inducer Of Acrosomal Ementioning

confidence: 99%

“…The ability of this motif to bind and activate heterotrimeric G-proteins is regulated by serine/threonine phosphorylation (Sun et al, 1995). In this regard, the cytoplasmic domain of surface GalT contains the predicted G-protein activation motif, and peptides corresponding to the cytoplasmic domain are able to bind PTx-sensitive G-protein subunits, whereas scrambled sequences are not (Gong et al, 1995). In Xenopus oocytes expressing GalT on their surface, mutagenesis of the G-protein activation motif in the GalT cytoplasmic domain eliminates G-protein activation in response to ZP3 or anti-GalT IgG (Shi et al, 2001) (Fig.…”

Section: Evidence Implicating Sperm Galt As An Inducer Of Acrosomal Ementioning

confidence: 99%

Reassessing the role of protein-carbohydrate complementarity during sperm-egg interactions in the mouse

Shur

2008

Int. J. Dev. Biol.

Self Cite

View full text Add to dashboard Cite

Despite years of intense study by many investigators, it may appear that we have made little progress towards a molecular understanding of mammalian sperm binding to the egg zona pellucida. An abundance of evidence derived from in vitro assays suggests that sperm-zona pellucida binding is dependent upon sperm recognition of specific glycan moieties on the zona pellucida glycoproteins. However, there is considerable disagreement regarding the identity of the zona pellucida sugars thought to mediate sperm binding, as well as disagreement over the identity of the sperm receptors themselves. Moreover, results from in vivo gene-targeting strategies fail to support a role for many, if not all, of the sperm receptors and their zona pellucida ligands implicated from in vitro assays. Nevertheless, a retrospective view of the literature suggests that some common principles are emerging regarding the molecular basis of mammalian sperm-zona binding, both with respect to the nature of the components that mediate binding, as well as the involvement of distinct receptor-ligand interactions, that involve both protein-and carbohydrate-dependent mechanisms of binding.

show abstract

Activation of a G Protein Complex by Aggregation of β-1,4-Galactosyltransferase on the Surface of Sperm

Cited by 156 publications

References 31 publications

Mechanism of Fertilization: A Modern View

Mechanism of Fertilization: A Modern View

Molecular characterization of neurohybrid cell death induced by Alzheimer's amyloid‐β peptides via p75NTR/PLAIDD

Reassessing the role of protein-carbohydrate complementarity during sperm-egg interactions in the mouse

Contact Info

Product

Resources

About