scholarly journals Adrenocorticotropic Hormone (ACTH) Responses Require Actions of the Melanocortin-2 Receptor Accessory Protein on the Extracellular Surface of the Plasma Membrane

2015 ◽  
Vol 290 (46) ◽  
pp. 27972-27985 ◽  
Author(s):  
Sundeep Malik ◽  
Terrance M. Dolan ◽  
Zachary J. Maben ◽  
Patricia M. Hinkle
2018 ◽  
Vol 3 (2) ◽  
pp. 314-323 ◽  
Author(s):  
Lucia Soletto ◽  
Sergio Hernández-Balfagó ◽  
Ana Rocha ◽  
Patrick Scheerer ◽  
Gunnar Kleinau ◽  
...  

2010 ◽  
Vol 84 (9) ◽  
pp. 4646-4658 ◽  
Author(s):  
Anja Habermann ◽  
Jacomine Krijnse-Locker ◽  
Heike Oberwinkler ◽  
Manon Eckhardt ◽  
Stefanie Homann ◽  
...  

ABSTRACT CD317/Bst-2/tetherin is a host factor that restricts the release of human immunodeficiency virus type 1 (HIV-1) by trapping virions at the plasma membrane of certain producer cells. It is antagonized by the HIV-1 accessory protein Vpu. Previous light microscopy studies localized CD317 to the plasma membrane and the endosomal compartment and showed Vpu induced downregulation. In the present study, we performed quantitative immunoelectron microscopy of CD317 in cells producing wild-type or Vpu-defective HIV-1 and in control cells. Double-labeling experiments revealed that CD317 localizes to the plasma membrane, to early and recycling endosomes, and to the trans-Golgi network. CD317 largely relocated to endosomes upon HIV-1 infection, and this effect was partly counteracted by Vpu. Unexpectedly, CD317 was enriched in the membrane of viral buds and cell-associated and cell-free viruses compared to the respective plasma membrane, and this enrichment was independent of Vpu. These results suggest that the tethering activity of CD317 critically depends on its density at the cell surface and appears to be less affected by its density in the virion membrane.


Endocrine ◽  
2018 ◽  
Vol 61 (1) ◽  
pp. 94-104 ◽  
Author(s):  
Jinye Liang ◽  
Lei Li ◽  
Xuanxuan Jin ◽  
Bingxin Xu ◽  
Linyu Pi ◽  
...  

2020 ◽  
Vol 102 (6) ◽  
pp. 1234-1247 ◽  
Author(s):  
Darius J Devlin ◽  
Smriti Agrawal Zaneveld ◽  
Kaori Nozawa ◽  
Xiao Han ◽  
Abigail R Moye ◽  
...  

Abstract Receptor accessory protein 6 (REEP6) is a member of the REEP/Ypt-interacting protein family that we recently identified as essential for normal endoplasmic reticulum homeostasis and protein trafficking in the retina of mice and humans. Interestingly, in addition to the loss of REEP6 in our knockout (KO) mouse model recapitulating the retinal degeneration of humans with REEP6 mutations causing retinitis pigmentosa (RP), we also found that male mice are sterile. Herein, we characterize the infertility caused by loss of Reep6. Expression of both Reep6 mRNA transcripts is present in the testis; however, isoform 1 becomes overexpressed during spermiogenesis. In vitro fertilization assays reveal that Reep6 KO spermatozoa are able to bind the zona pellucida but are only able to fertilize oocytes lacking the zona pellucida. Although spermatogenesis appears normal in KO mice, cauda epididymal spermatozoa have severe motility defects and variable morphological abnormalities, including bent or absent tails. Immunofluorescent staining reveals that REEP6 expression first appears in stage IV tubules within step 15 spermatids, and REEP6 localizes to the connecting piece, midpiece, and annulus of mature spermatozoa. These data reveal an important role for REEP6 in sperm motility and morphology and is the first reported function for a REEP protein in reproductive processes. Additionally, this work identifies a new gene potentially responsible for human infertility and has implications for patients with RP harboring mutations in REEP6.


Diabetes ◽  
2017 ◽  
Vol 67 (2) ◽  
pp. 222-234 ◽  
Author(s):  
Xiaodong Zhang ◽  
Alicia M. Saarinen ◽  
Latoya E. Campbell ◽  
Elena A. De Filippis ◽  
Jun Liu

2007 ◽  
Vol 104 (47) ◽  
pp. 18660-18665 ◽  
Author(s):  
S. Ali ◽  
M. Huber ◽  
C. Kollewe ◽  
S. C. Bischoff ◽  
W. Falk ◽  
...  

Hepatology ◽  
2007 ◽  
Vol 47 (1) ◽  
pp. 268-278 ◽  
Author(s):  
Coen C. Paulusma ◽  
Dineke E. Folmer ◽  
Kam S. Ho-Mok ◽  
D. Rudi de Waart ◽  
Petra M. Hilarius ◽  
...  

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