Endosomal sorting complex required for transport proteins in cancer pathogenesis, vesicular transport, and non-endosomal functions

2008 ◽  
Vol 99 (7) ◽  
pp. 1293-1303 ◽  
Author(s):  
Nobuyuki Tanaka ◽  
Masanao Kyuuma ◽  
Kazuo Sugamura
Keyword(s):  
Vesicular Transport ◽  
Transport Proteins ◽  
Endosomal Sorting ◽  
Cancer Pathogenesis

ESCRT proteins and the regulation of endocytic delivery to lysosomes

2009 ◽  
Vol 37 (1) ◽  
pp. 178-180 ◽  
Author(s):  
J. Paul Luzio ◽  
Siân C. Piper ◽  
Katherine Bowers ◽  
Michael D.J. Parkinson ◽  
Paul J. Lehner ◽  
...  
Keyword(s):  
Cell Surface ◽  
Mhc Class I ◽  
Mammalian Cells ◽  
Transport Proteins ◽  
Class I ◽  
Multivesicular Bodies ◽  
Down Regulation ◽  
Morphological Effect ◽  
Endosomal Sorting ◽  
Endocytic Compartments

In mammalian cells, there is evidence of cargo specificity in the requirement for particular ESCRT (endosomal sorting complex required for transport) proteins to sort cargo into the luminal vesicles of MVBs (multivesicular bodies). We have focussed on studying the ESCRT requirements for delivery of MHC class I to lysosomes following polyubiquitination by the Kaposi's sarcoma-associated herpesvirus protein K3. Down-regulation of polyubiquitinated cell-surface MHC class I in HeLa cells stably expressing K3 is achieved via clathrin-mediated endocytosis, followed by sorting into the luminal vesicles of MVBs and eventual delivery to lysosomes. Depletion of ESCRT-I and some ESCRT-III components interferes with this sorting and allows recycling of MHC class I to the cell surface. Depletion of ESCRT-II components has no effect on K3-mediated down-regulation of MHC class I and no gross morphological effect on endocytic compartments. Thus virally polyubiquitinated MHC class I does not require all of the ESCRT proteins in order to be sorted into the luminal vesicles of MVBs. However, there may be a further requirement for ESCRT-III proteins to ensure the efficient fusion of MVBs with lysosomes.

scholarly journals Computational identification of vesicular transport proteins from sequences using deep gated recurrent units architecture

2019 ◽  
Vol 17 ◽  
pp. 1245-1254 ◽  
Author(s):  
Nguyen Quoc Khanh Le ◽  
Edward Kien Yee Yapp ◽  
N. Nagasundaram ◽  
Matthew Chin Heng Chua ◽  
Hui-Yuan Yeh
Keyword(s):  
Vesicular Transport ◽  
Transport Proteins ◽  
Computational Identification ◽  
Gated Recurrent Units

scholarly journals KRAS regulation by small non-coding RNAs and SNARE proteins

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Yonglu Che ◽  
Zurab Siprashvili ◽  
Joanna R. Kovalski ◽  
Tiffany Jiang ◽  
Glenn Wozniak ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Growth Factor ◽  
Vesicular Transport ◽  
Transport Proteins ◽  
Protein Labeling ◽  
Snare Proteins ◽  
Wild Type ◽  
Downstream Effectors ◽  
Therapeutic Opportunity ◽  
Non Coding Rnas

Abstract KRAS receives and relays signals at the plasma membrane (PM) where it transmits extracellular growth factor signals to downstream effectors. SNORD50A/B were recently found to bind KRAS and inhibit its tumorigenic action by unknown mechanisms. KRAS proximity protein labeling was therefore undertaken in SNORD50A/B wild-type and knockout cells, revealing that SNORD50A/B RNAs shape the composition of proteins proximal to KRAS, notably by inhibiting KRAS proximity to the SNARE vesicular transport proteins SNAP23, SNAP29, and VAMP3. To remain enriched on the PM, KRAS undergoes cycles of endocytosis, solubilization, and vesicular transport to the PM. Here we report that SNAREs are essential for the final step of this process, with KRAS localization to the PM facilitated by SNAREs but antagonized by SNORD50A/B. Antagonism between SNORD50A/B RNAs and specific SNARE proteins thus controls KRAS localization, signaling, and tumorigenesis, and disrupting SNARE-enabled KRAS function represents a potential therapeutic opportunity in KRAS-driven cancer.

scholarly journals VTP-Identifier: Vesicular Transport Proteins Identification Based on PSSM Profiles and XGBoost

2022 ◽  
Vol 12 ◽  
Author(s):  
Yue Gong ◽  
Benzhi Dong ◽  
Zixiao Zhang ◽  
Yixiao Zhai ◽  
Bo Gao ◽  
...  
Keyword(s):  
Protein Function ◽  
Protein Function Prediction ◽  
Transition Probability ◽  
Vesicular Transport ◽  
Transport Proteins ◽  
Data Set ◽  
Other Information ◽  
Scoring Matrix ◽  
Test Sets ◽  
Matthew’S Correlation Coefficient

Vesicular transport proteins are related to many human diseases, and they threaten human health when they undergo pathological changes. Protein function prediction has been one of the most in-depth topics in bioinformatics. In this work, we developed a useful tool to identify vesicular transport proteins. Our strategy is to extract transition probability composition, autocovariance transformation and other information from the position-specific scoring matrix as feature vectors. EditedNearesNeighbours (ENN) is used to address the imbalance of the data set, and the Max-Relevance-Max-Distance (MRMD) algorithm is adopted to reduce the dimension of the feature vector. We used 5-fold cross-validation and independent test sets to evaluate our model. On the test set, VTP-Identifier presented a higher performance compared with GRU. The accuracy, Matthew’s correlation coefficient (MCC) and area under the ROC curve (AUC) were 83.6%, 0.531 and 0.873, respectively.

Effects of Vincristine on Endothelial Microtubules in the Spinal Cord

1976 ◽  
Vol 34 ◽  
pp. 58-59
Author(s):  
John L. Beggs ◽  
John D. Waggener ◽  
Wanda Miller
Keyword(s):  
Spinal Cord ◽  
Biological Activity ◽  
Horseradish Peroxidase ◽  
Transport Mechanism ◽  
Vasogenic Edema ◽  
Vesicular Transport ◽  
Close Proximity

Microtubules (MT) are versatile organelles participating in a wide variety of biological activity. MT involvement in the movement and transport of cytoplasmic components has been well documented. In the course of our study on trauma-induced vasogenic edema in the spinal cord we have concluded that endothelial vesicles contribute to the edema process. Using horseradish peroxidase as a vascular tracer, labeled endothelial vesicles were present in all situations expected if a vesicular transport mechanism was in operation. Frequently,labeled vesicles coalesced to form channels that appeared to traverse the endothelium. The presence of MT in close proximity to labeled vesicles sugg ested that MT may play a role in vesicular activity.

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