Quantifying Compartment-Specific Protein Translocation in Astrocytes by Object-Oriented Image Analysis: Mitochondrial Translocation of PKCδ

Author(s):  
Kiavasch Mohammad Nejad Farid ◽  
Amin Derouiche
2019 ◽  
Vol 116 (4) ◽  
pp. 1299-1308 ◽  
Author(s):  
Christopher P. Walczak ◽  
Dara E. Leto ◽  
Lichao Zhang ◽  
Celeste Riepe ◽  
Ryan Y. Muller ◽  
...  

Ubiquitin fold modifier 1 (UFM1) is a small, metazoan-specific, ubiquitin-like protein modifier that is essential for embryonic development. Although loss-of-function mutations in UFM1 conjugation are linked to endoplasmic reticulum (ER) stress, neither the biological function nor the relevant cellular targets of this protein modifier are known. Here, we show that a largely uncharacterized ribosomal protein, RPL26, is the principal target of UFM1 conjugation. RPL26 UFMylation and de-UFMylation is catalyzed by enzyme complexes tethered to the cytoplasmic surface of the ER and UFMylated RPL26 is highly enriched on ER membrane-bound ribosomes and polysomes. Biochemical analysis and structural modeling establish that UFMylated RPL26 and the UFMylation machinery are in close proximity to the SEC61 translocon, suggesting that this modification plays a direct role in cotranslational protein translocation into the ER. These data suggest that UFMylation is a ribosomal modification specialized to facilitate metazoan-specific protein biogenesis at the ER.


2006 ◽  
Vol 188 (4) ◽  
pp. 1251-1259 ◽  
Author(s):  
Nicholas J. Hand ◽  
Reinhard Klein ◽  
Anke Laskewitz ◽  
Mechthild Pohlschröder

ABSTRACT The majority of secretory proteins are translocated into and across hydrophobic membranes via the universally conserved Sec pore. Accessory proteins, including the SecDF-YajC Escherichia coli membrane complex, are required for efficient protein secretion. E. coli SecDF-YajC has been proposed to be involved in the membrane cycling of SecA, the cytoplasmic bacterial translocation ATPase, and in the stabilizing of SecG, a subunit of the Sec pore. While there are no identified archaeal homologs of either SecA or SecG, many archaea possess homologs of SecD and SecF. Here, we present the first study that addresses the function of archaeal SecD and SecF homologs. We show that the SecD and SecF components in the model archaeon Haloferax volcanii form a cytoplasmic membrane complex in the native host. Furthermore, as in E. coli, an H. volcanii ΔsecFD mutant strain exhibits both severe cold sensitivity and a Sec-specific protein translocation defect. Taken together, these results demonstrate significant functional conservation among the prokaryotic SecD and SecF homologs despite the distinct composition of their translocation machineries.


2015 ◽  
Vol 7 (4) ◽  
pp. 4318-4342 ◽  
Author(s):  
Jie Dou ◽  
Kuan-Tsung Chang ◽  
Shuisen Chen ◽  
Ali Yunus ◽  
Jin-King Liu ◽  
...  

2012 ◽  
Vol 9 (2) ◽  
pp. 239-247
Author(s):  
Kazuyuki Takahashi ◽  
Noritoshi Kamagata ◽  
Keitarou Hara

1987 ◽  
Author(s):  
Thomas C. Rearick

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