ArticleAmerican journal of physiology. Cell physiology2008
mCLCA4 ER processing and secretion requires luminal sorting motifs.
Article in American journal of physiology. Cell physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- A transcriptomic study of myogenic differentiation under the overexpression of PPARγ by RNA-Seq.Scientific reports · 2017Article
- Two di-leucine motifs regulate trafficking and function of mouse ASIC2a.Molecular brain · 2016Article
- Emerging genetic basis of osteochondritis dissecans.Clinics in sports medicine · 2014Review
- Self-cleavage of human CLCA1 protein by a novel internal metalloprotease domain controls calcium-activated chloride channel activation.The Journal of biological chemistry · 2012Article
- IL-13-induced airway mucus production is attenuated by MAPK13 inhibition.The Journal of clinical investigation · 2012Article
- hCLCA2 Is a p53-Inducible Inhibitor of Breast Cancer Cell Proliferation.Cancer research · 2009Article
- The role of CLCA proteins in inflammatory airway disease.Annual review of physiology · 2009Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Ca(+)-activated Cl(-) channel (CLCA) proteins are encoded by a family of highly related and clustered genes in mammals that are markedly upregulated in inflammation and have been shown to affect chloride transport. Here we describe the cellular processing and regulatory sequences underlying murine (m) CLCA4 proteins. The 125-kDa mCLCA4 gene product is cleaved to 90- and 40-kDa fragments, and the NH(2)- and COOH-terminal fragments are secreted, where they are found in cell media and associated with the plasma membrane. The 125-kDa full-length protein is only found in the endoplasmic reticulum (ER), and specific luminal diarginine retention and dileucine forward trafficking signals contained within the CLCA4 sequence regulate export from the ER and proteolytic processing. Mutation of the dileucine luminal sequences resulted in ER trapping of the immaturely glycosylated 125-kDa peptide, indicating that proteolytic cleavage occurs following recognition of the trafficking motifs. Moreover, the mutated dileucine and diarginine signal sequences directed processing of a secreted form of enhanced green fluorescent protein in a manner consistent with the effects on mCLCA4.
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Registered trials
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