RRC ID 34909
Author Uematsu S, Goto Y, Suzuki T, Sasazawa Y, Dohmae N, Simizu S.
Title N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis.
Journal FEBS Open Bio
Abstract Extracellular matrix protein 1 (ECM1) is expressed in a wide variety of tissues and plays important roles in extracellular matrix formation. Additionally, ECM1 gene mutations cause lipoid proteinosis (LP), a rare skin condition of genetic origin. However, an effective therapeutic approach of LP is not established. Here, we showed that ECM1 gene mutation observed in LP patients significantly suppresses its secretion. As ECM1 has three putative N-glycosylation sites and most of mutated ECM1 observed in LP patients are defective in these N-glycosylation sites, we investigated the correlation between LP and N-glycosylation of ECM1. We identified that the Asn(354) and Asn(444) residues in ECM1 were N-glycosylated by mass spectrometry analysis. In addition, an N-linked glycan at Asn(354) negatively regulated secretion of ECM1, contrary to LP patient-derived mutants. These results indicate that the defect of N-glycosylation in ECM1 is not involved in the aberration of secretion of LP-derived mutated ECM1.
Volume 4
Pages 879-85
Published 2014-1-1
DOI 10.1016/j.fob.2014.10.004
PII S2211-5463(14)00093-X
PMID 25379385
PMC PMC4215116
IF 2.231
Times Cited 10
DNA material pCI-ECM1 (RDB13302) pCI-ECM1-Q276X (RDB13303) pCI-ECM1-W359X (RDB13304) pCI-ECM1-N354Q (RDB13305) pCI-ECM1-N444Q (RDB13306).