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ErbB-4 and TNF-alpha converting enzyme localization to membrane microdomains
Journal article   Peer reviewed

ErbB-4 and TNF-alpha converting enzyme localization to membrane microdomains

Kristina W. Thiel and Graham Carpenter
Biochemical and biophysical research communications, Vol.350(3), pp.629-633
11/24/2006
DOI: 10.1016/j.bbrc.2006.09.095
PMCID: PMC1637093
PMID: 17027649
url
https://www.ncbi.nlm.nih.gov/pmc/articles/1637093View
Open Access

Abstract

Sequential proteolytic processing of ErbB-4 occurs in response to ligand addition. Here, we assess the localization of cleavable and non-cleavable ErbB-4 isoforms to membrane microdomains using three methodologies: (1) Triton X-100-insolubility, (2) Brij98-insolubility, and (3) detergent-free density gradient centrifugation. Whereas ErbB-4 translocated to a Triton X-100-insoluble fraction upon treatment of T47D cells with heregulin, it constitutively associated with a Brij98-insoluble fraction and a lipid raft fraction isolated using detergent-free methodology. Comparison of cleavable and non-cleavable isoforms of ErbB-4 revealed that both ErbB-4 isoforms are constitutively localized to either a Triton X-100-soluble or Brij98-insoluble fraction. In contrast, addition of heregulin resulted in translocation of the cleavable isoform to a detergent-free lipid raft. Tumor necrosis factor-a converting enzyme (TACE), the ectodomain secretase for ErbB-4. was present predominantly in its mature active form in most microdomains analyzed. These data suggest the assembly of ErbB-4 ectodomain cleavage apparatus in a membrane microdomain. (c) 2006 Elsevier Inc. All rights reserved.
Biochemistry & Molecular Biology Biophysics Life Sciences & Biomedicine Science & Technology

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