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2015 ; 112
(49
): E6752-61
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ER trapping reveals Golgi enzymes continually revisit the ER through a recycling
pathway that controls Golgi organization
#MMPMID26598700
Sengupta P
; Satpute-Krishnan P
; Seo AY
; Burnette DT
; Patterson GH
; Lippincott-Schwartz J
Proc Natl Acad Sci U S A
2015[Dec]; 112
(49
): E6752-61
PMID26598700
show ga
Whether Golgi enzymes remain localized within the Golgi or constitutively cycle
through the endoplasmic reticulum (ER) is unclear, yet is important for
understanding Golgi dependence on the ER. Here, we demonstrate that the
previously reported inefficient ER trapping of Golgi enzymes in a rapamycin-based
assay results from an artifact involving an endogenous ER-localized 13-kD FK506
binding protein (FKBP13) competing with the FKBP12-tagged Golgi enzyme for
binding to an FKBP-rapamycin binding domain (FRB)-tagged ER trap. When we express
an FKBP12-tagged ER trap and FRB-tagged Golgi enzymes, conditions precluding such
competition, the Golgi enzymes completely redistribute to the ER upon rapamycin
treatment. A photoactivatable FRB-Golgi enzyme, highlighted only in the Golgi,
likewise redistributes to the ER. These data establish Golgi enzymes
constitutively cycle through the ER. Using our trapping scheme, we identify roles
of rab6a and calcium-independent phospholipase A2 (iPLA2) in Golgi enzyme
recycling, and show that retrograde transport of Golgi membrane underlies Golgi
dispersal during microtubule depolymerization and mitosis.