2021
DOI: 10.1371/journal.pbio.3001117
|View full text |Cite
|
Sign up to set email alerts
|

Correction: Membrane progesterone receptor induces meiosis in Xenopus oocytes through endocytosis into signaling endosomes and interaction with APPL1 and Akt2

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
6
0

Year Published

2021
2021
2023
2023

Publication Types

Select...
6

Relationship

0
6

Authors

Journals

citations
Cited by 7 publications
(6 citation statements)
references
References 1 publication
0
6
0
Order By: Relevance
“…More recent structural analyses suggest the N-terminal of mPRs is intracellular [ 20 , 27 ], which is supported by the recent prediction of the “positive-inside rule” in which higher proportions of positively charged amino acids are intracellular [ 21 ]. This orientation is supported by results using Xenopus mPRβ clones with N- terminal fluorescent tags under permeabilized and nonpermeabilized conditions [ 25 ]. The C-terminal domain of mPRs is longer than that of the AdipoRs and is predicted to form an eighth TM domain with an intracellular C-terminal [ 20 , 27 ].…”
Section: Cellular Distribution and Membrane Topologymentioning
confidence: 71%
See 4 more Smart Citations
“…More recent structural analyses suggest the N-terminal of mPRs is intracellular [ 20 , 27 ], which is supported by the recent prediction of the “positive-inside rule” in which higher proportions of positively charged amino acids are intracellular [ 21 ]. This orientation is supported by results using Xenopus mPRβ clones with N- terminal fluorescent tags under permeabilized and nonpermeabilized conditions [ 25 ]. The C-terminal domain of mPRs is longer than that of the AdipoRs and is predicted to form an eighth TM domain with an intracellular C-terminal [ 20 , 27 ].…”
Section: Cellular Distribution and Membrane Topologymentioning
confidence: 71%
“…Localization of mPRs in this region is not unexpected since membrane receptors are trafficked to the cell membrane from the endoplasmic reticulum, which usually retains most of the receptor protein [ 23 ]. After ligand binding, mPRs are rapidly internalized by a clathrin-dependent mechanism [ 24 , 25 ], resulting in decreased cell-surface expression of the receptor, which is slowly restored [ 24 ]. The restoration of mPRs on the cell surface involves the participation of various adaptor proteins.…”
Section: Cellular Distribution and Membrane Topologymentioning
confidence: 99%
See 3 more Smart Citations