Unknown

Dataset Information

0

Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI.


ABSTRACT: Glycosylphosphatidylinositol (GPI) anchoring of proteins is a posttranslational modification occurring in the endoplasmic reticulum (ER). After GPI attachment, proteins are transported by coat protein complex II (COPII)-coated vesicles from the ER. Because GPI-anchored proteins (GPI-APs) are localized in the lumen, they cannot interact with cytosolic COPII components directly. Receptors that link GPI-APs to COPII are thought to be involved in efficient packaging of GPI-APs into vesicles; however, mechanisms of GPI-AP sorting are not well understood. Here we describe two remodeling reactions for GPI anchors, mediated by PGAP1 and PGAP5, which were required for sorting of GPI-APs to ER exit sites. The p24 family of proteins recognized the remodeled GPI-APs and sorted them into COPII vesicles. Association of p24 proteins with GPI-APs was pH dependent, which suggests that they bind in the ER and dissociate in post-ER acidic compartments. Our results indicate that p24 complexes act as cargo receptors for correctly remodeled GPI-APs to be sorted into COPII vesicles.

SUBMITTER: Fujita M 

PROVIDER: S-EPMC3135397 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI.

Fujita Morihisa M   Watanabe Reika R   Jaensch Nina N   Romanova-Michaelides Maria M   Satoh Tadashi T   Kato Masaki M   Riezman Howard H   Yamaguchi Yoshiki Y   Maeda Yusuke Y   Kinoshita Taroh T  

The Journal of cell biology 20110704 1


Glycosylphosphatidylinositol (GPI) anchoring of proteins is a posttranslational modification occurring in the endoplasmic reticulum (ER). After GPI attachment, proteins are transported by coat protein complex II (COPII)-coated vesicles from the ER. Because GPI-anchored proteins (GPI-APs) are localized in the lumen, they cannot interact with cytosolic COPII components directly. Receptors that link GPI-APs to COPII are thought to be involved in efficient packaging of GPI-APs into vesicles; however  ...[more]

Similar Datasets

| S-EPMC4915193 | biostudies-literature
| S-EPMC11298655 | biostudies-literature
| S-EPMC4121523 | biostudies-literature
| S-EPMC6541436 | biostudies-literature
| S-EPMC7732199 | biostudies-literature
| S-EPMC4689344 | biostudies-literature
| S-EPMC2765922 | biostudies-literature
| S-EPMC9520029 | biostudies-literature
| S-EPMC9997660 | biostudies-literature
| S-EPMC3154887 | biostudies-literature