Electron microscopic characterization of nuclear egress in the sea urchin gastrula.

J Morphol

Department of Biology, College of Staten Island, City University of New York, Staten Island, New York, United States of America.

Published: May 2018

Nuclear egress, also referred to as nuclear envelope (NE) budding, is a process of transport in which vesicles containing molecular complexes or viral particles leave the nucleus through budding from the inner nuclear membrane (INM) to enter the perinuclear space. Following this event, the perinuclear vesicles (PNVs) fuse with the outer nuclear membrane (ONM), where they release their contents into the cytoplasm. Nuclear egress is thought to participate in many functions such as viral replication, cellular differentiation, and synaptic development. The molecular basis for nuclear egress is now beginning to be elucidated. Here, we observe in the sea urchin gastrula, using serial section transmission electron microscopy, strikingly abundant PNVs containing as yet unidentified granules that resemble the ribonucleoprotein complexes (RNPs) previously observed in similar types of PNVs. Some PNVs were observed in the process of fusion with the ONM where they appeared to release their contents into the cytoplasm. These vesicles were abundantly observed in all three presumptive germ layers. These findings indicate that nuclear egress is likely to be an important mechanism for nucleocytoplasmic transfer during sea urchin development. The sea urchin may be a useful model to characterize further and gain a better understanding of the process of nuclear egress.

Download full-text PDF

Source
http://dx.doi.org/10.1002/jmor.20796DOI Listing

Publication Analysis

Top Keywords

nuclear egress
24
sea urchin
16
nuclear
9
urchin gastrula
8
nuclear membrane
8
release contents
8
contents cytoplasm
8
egress
6
electron microscopic
4
microscopic characterization
4

Similar Publications

Background/objective: The Rs1 exon-1-del rat (Rs1KO) XLRS model shows normal retinal development until postnatal day 12 (P12) when small cystic spaces start to form in the inner nuclear layer. These spaces enlarge rapidly, peak at P15, and then collapse by P19.

Methods: We explored the possible involvement of Kir4.

View Article and Find Full Text PDF

Identification and subcellular localization of proteins that interact with Duck plague virus pUL14 in infected host cells.

Poult Sci

December 2024

Institute of Veterinary Medicine and Immunology, Sichuan Agricultural University, Chengdu 611130, PR China; Key Laboratory of Animal Disease and Human Health of Sichuan Province, Chengdu 611130, PR China; International Joint Research Center for Animal Disease Prevention and Control of Sichuan Province, Chengdu 611130, PR China; Engineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of Education of the People's Republic of China, Chengdu 611130, PR China; Research Center of Avian Disease, College of Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, PR China.

Duck plague (DP), which is caused by duck plague virus (DPV), is an infectious disease that severely harms the waterfowl breeding industry. The UL14 protein (pUL14) is a tegument protein encoded by the UL14 gene, which is located in the unique long (UL) region of the DPV genome. DPV pUL14 plays a crucial role in viral replication, likely by interacting with host and viral proteins that have yet to be identified.

View Article and Find Full Text PDF

The nuclear-cytoplasmic trafficking of matrix proteins (M) is essential for henipavirus budding, with M protein ubiquitination playing a pivotal role in this dynamic process. Despite its importance, the intricacies of the M ubiquitination cascade have remained elusive. In this study, we elucidate a novel mechanism by which Nipah virus (NiV), a highly pathogenic henipavirus, utilizes a ubiquitination complex involving the E2 ubiquitin-conjugating enzyme RAD6A and the E3 ubiquitin ligase RAD18 to ubiquitinate the virus's M protein, thereby facilitating its nuclear-cytoplasmic trafficking.

View Article and Find Full Text PDF

Autographa californica multiple nucleopolyhedrovirus (AcMNPV) () is highly conserved in baculoviruses. Previous studies have shown that is required for the production of infectious budded virions (BVs). However, the functional role of in virion morphogenesis remains unknown.

View Article and Find Full Text PDF

CLCC1 promotes membrane fusion during herpesvirus nuclear egress.

bioRxiv

September 2024

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts, United States of America.

Article Synopsis
  • Researchers studied how ancient viruses, like herpes, move their protective capsids from the nucleus to the cytoplasm in infected cells.
  • They found that these viruses use a process involving a host protein called CLCC1, crucial for the fusion of capsids with the inner nuclear membrane.
  • The absence of CLCC1 hampers viral spread and leads to problems within the cell's structures, indicating that viruses have evolved to exploit ancient cellular mechanisms for their transmission.
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!