Research output: Contribution to journal › Article › peer-review
Post-ER Stress Biogenesis of Golgi Is Governed by Giantin. / Frisbie, Cole P.; Lushnikov, Alexander Y.; Krasnoslobodtsev, Alexey V.; Riethoven, Jean Jack M.; Clarke, Jennifer L.; Stepchenkova, Elena I.; Petrosyan, Armen.
In: Cells, Vol. 8, No. 12, 13.12.2019.Research output: Contribution to journal › Article › peer-review
}
TY - JOUR
T1 - Post-ER Stress Biogenesis of Golgi Is Governed by Giantin
AU - Frisbie, Cole P.
AU - Lushnikov, Alexander Y.
AU - Krasnoslobodtsev, Alexey V.
AU - Riethoven, Jean Jack M.
AU - Clarke, Jennifer L.
AU - Stepchenkova, Elena I.
AU - Petrosyan, Armen
PY - 2019/12/13
Y1 - 2019/12/13
N2 - BACKGROUND: The Golgi apparatus undergoes disorganization in response to stress, but it is able to restore compact and perinuclear structure under recovery. This self-organization mechanism is significant for cellular homeostasis, but remains mostly elusive, as does the role of giantin, the largest Golgi matrix dimeric protein. METHODS: In HeLa and different prostate cancer cells, we used the model of cellular stress induced by Brefeldin A (BFA). The conformational structure of giantin was assessed by proximity ligation assay and atomic force microscopy. The post-BFA distribution of Golgi resident enzymes was examined by 3D SIM high-resolution microscopy. RESULTS: We detected that giantin is rather flexible than an extended coiled-coil dimer and BFA-induced Golgi disassembly was associated with giantin monomerization. A fusion of the nascent Golgi membranes after BFA washout is forced by giantin re-dimerization via disulfide bond in its luminal domain and assisted by Rab6a GTPase. GM130-GRASP65-dependent enzymes are able to reach the nascent Golgi membranes, while giantin-sensitive enzymes appeared at the Golgi after its complete recovery via direct interaction of their cytoplasmic tail with N-terminus of giantin. CONCLUSION: Post-stress recovery of Golgi is conducted by giantin dimer and Golgi proteins refill membranes according to their docking affiliation rather than their intra-Golgi location.
AB - BACKGROUND: The Golgi apparatus undergoes disorganization in response to stress, but it is able to restore compact and perinuclear structure under recovery. This self-organization mechanism is significant for cellular homeostasis, but remains mostly elusive, as does the role of giantin, the largest Golgi matrix dimeric protein. METHODS: In HeLa and different prostate cancer cells, we used the model of cellular stress induced by Brefeldin A (BFA). The conformational structure of giantin was assessed by proximity ligation assay and atomic force microscopy. The post-BFA distribution of Golgi resident enzymes was examined by 3D SIM high-resolution microscopy. RESULTS: We detected that giantin is rather flexible than an extended coiled-coil dimer and BFA-induced Golgi disassembly was associated with giantin monomerization. A fusion of the nascent Golgi membranes after BFA washout is forced by giantin re-dimerization via disulfide bond in its luminal domain and assisted by Rab6a GTPase. GM130-GRASP65-dependent enzymes are able to reach the nascent Golgi membranes, while giantin-sensitive enzymes appeared at the Golgi after its complete recovery via direct interaction of their cytoplasmic tail with N-terminus of giantin. CONCLUSION: Post-stress recovery of Golgi is conducted by giantin dimer and Golgi proteins refill membranes according to their docking affiliation rather than their intra-Golgi location.
KW - Brefeldin A
KW - giantin
KW - Golgi biogenesis
KW - GRASP65
KW - Rab6a
UR - http://www.scopus.com/inward/record.url?scp=85090170658&partnerID=8YFLogxK
U2 - 10.3390/cells8121631
DO - 10.3390/cells8121631
M3 - Article
C2 - 31847122
AN - SCOPUS:85090170658
VL - 8
JO - Cells
JF - Cells
SN - 2073-4409
IS - 12
ER -
ID: 88539933