ArticleThe Biochemical journal2003
Retrieval-independent localization of lysyl hydroxylase in the endoplasmic reticulum via a peptide fold in its iron-binding domain.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Dietary iron intake and its impact on osteopenia/osteoporosis.BMC endocrine disorders · 2023Article
- Collagen beta (1-Bioscience reports · 2017Article
- Decoupling ferritin synthesis from free cytosolic iron results in ferritin secretion.Cell metabolism · 2011Article
- Genomic structure and embryonic expression of zebrafish lysyl hydroxylase 1 and lysyl hydroxylase 2.Matrix biology : journal of the International Society for Matrix Biology · 2007Article
- NCB5OR is a novel soluble NAD(P)H reductase localized in the endoplasmic reticulum.The Journal of biological chemistry · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysyl hydroxylase (LH) is a peripheral membrane protein in the lumen of the endoplasmic reticulum (ER) that catalyses hydroxylation of lysine residues in collagenous sequences. Previously, we have mapped its primary ER localization motif within a 40-amino acid segment at its C-terminus. Here, we have characterized this localization mechanism in more detail, and our results indicate that this segment confers ER residency in a KDEL-receptor-independent manner, and without any apparent recycling of the enzyme between the Golgi apparatus and the ER. In addition, we show that a rather long peptide region, rather than a specific peptide sequence per se, is required for efficient retention of a reporter protein in the ER. Accordingly, the minimal retention motif was found to require the last 32 C-terminal amino acids, and sequential substitution of all five charged residues within this critical segment interfered only marginally with the retention or association of the enzyme with the ER membranes. Moreover, our fold-recognition and structure-prediction analyses suggested that this critical peptide segment forms an extended loop within LH's iron-binding domain, and that this loop is exposed and readily accessible for binding. Collectively, our results define a novel retrieval-independent retention mechanism in the ER.
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Registered trials
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