Subcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail Anchor.
The canonical protein tyrosine phosphatase PTP1B is an important regulator of diverse cellular signaling networks. PTP1B has long been thought to exert its influence solely from its perch on the endoplasmic reticulum (ER); however, an additional subpopulation of PTP1B has recently been detected in m...
Main Authors: | Julia Fueller, Mikhail V Egorov, Kirstin A Walther, Ola Sabet, Jana Mallah, Markus Grabenbauer, Ali Kinkhabwala |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4592070?pdf=render |
Similar Items
-
Correction: Subcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail Anchor.
by: Julia Fueller, et al.
Published: (2016-01-01) -
Regulation of signaling at regions of cell-cell contact by endoplasmic reticulum-bound protein-tyrosine phosphatase 1B.
by: Fawaz G Haj, et al.
Published: (2012-01-01) -
Metabolic interplay between peroxisomes and other subcellular organelles including mitochondria and the endoplasmic reticulum
by: Ronald J.A. Wanders, et al.
Published: (2016-01-01) -
Endoplasmic Reticulum Export of GPI-Anchored Proteins
by: Sergio Lopez, et al.
Published: (2019-07-01) -
Endoplasmic Reticulum–Mitochondria Contact Sites and Neurodegeneration
by: Lingna Xu, et al.
Published: (2020-06-01)