Human SND2 mediates ER targeting of GPI‐anchored proteins with low hydrophobic GPI attachment signals

Over 100 glycosylphosphatidylinositol‐anchored proteins (GPI‐APs) are encoded in the mammalian genome. It is not well understood how these proteins are targeted and translocated to the endoplasmic reticulum (ER). Here, we reveal that many GPI‐APs, such as CD59, CD55, and CD109, utilize human SND2 (h...

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Veröffentlicht in:	FEBS letters 2021-06, Vol.595 (11), p.1542-1558
Hauptverfasser:	Yang, Jing, Hirata, Tetsuya, Liu, Yi‐Shi, Guo, Xin‐Yu, Gao, Xiao‐Dong, Kinoshita, Taroh, Fujita, Morihisa, Sonnino, Sandro
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Sprache:	eng
Schlagworte:	endoplasmic reticulum glycosylphosphatidylinositol protein targeting signal recognition particle SND2
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creator	Yang, Jing Hirata, Tetsuya Liu, Yi‐Shi Guo, Xin‐Yu Gao, Xiao‐Dong Kinoshita, Taroh Fujita, Morihisa Sonnino, Sandro
description	Over 100 glycosylphosphatidylinositol‐anchored proteins (GPI‐APs) are encoded in the mammalian genome. It is not well understood how these proteins are targeted and translocated to the endoplasmic reticulum (ER). Here, we reveal that many GPI‐APs, such as CD59, CD55, and CD109, utilize human SND2 (hSND2)‐dependent ER targeting machinery. We also found that signal recognition particle receptors seem to cooperate with hSND2 to target GPI‐APs to the ER. Both the N‐terminal signal sequence and C‐terminal GPI attachment signal of GPI‐APs contribute to ER targeting via the hSND2‐dependent pathway. Particularly, the hydrophobicity of the C‐terminal GPI attachment signal acts as the determinant of hSND2 dependency. Our results explain the route and mechanism of the ER targeting of GPI‐APs in mammalian cells.
doi_str_mv	10.1002/1873-3468.14083
format	Article
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source	Wiley Online Library; Wiley Online Library (Open Access Collection); Alma/SFX Local Collection; EZB Electronic Journals Library
subjects	endoplasmic reticulum glycosylphosphatidylinositol protein targeting signal recognition particle SND2
title	Human SND2 mediates ER targeting of GPI‐anchored proteins with low hydrophobic GPI attachment signals
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