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60S ribosomal protein L35 regulates β-casein translational elongation and secretion in bovine mammary epithelial cells.

Abstract：

:60S ribosomal protein L35 (RPL35) is an important component of the 60S ribosomal subunit and has a role in protein translation and endoplasmic reticulum (ER) docking. However, few studies have investigated RPL35 in eukaryotes and much remains to be learned. Here, we analyzed the function of RPL35 in β-casein (CSN2) synthesis and secretion in bovine mammary epithelial cells (BMECs). We found that methionine (Met) could promote the expressions of CSN2 and RPL35. Analysis of overexpression and inhibition of RPL35 confirmed that it could mediate the Met signal and regulate CSN2 expression. The mechanism of CSN2 regulation by RPL35 was analyzed by coimmunoprecipitation (Co-IP), colocalization, fluorescence resonance energy transfer (FRET) and gene mutation. We found that RPL35 could control ribosome translational elongation during synthesis of CSN2 by interacting with eukaryotic translational elongation factor 2 (eEF2), and that eEF2 was the signaling molecule downstream of RPL35 controlling this process. RPL35 could also control the secretion of CSN2 by locating it to the ER. Taken together, these results revealed that, RPL35 was an important positive regulatory factor involving in the Met-mediated regulation of CSN2 translational elongation and secretion.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Jiang N,Hu L,Liu C,Gao X,Zheng S

doi

10.1016/j.abb.2015.08.006

subject

Has Abstract

pub_date

2015-10-01 00:00:00

pages

130-9

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(15)30032-1

journal_volume

583

pub_type

杂志文章

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