PMID- 10484778
OWN - NLM
STAT- MEDLINE
DCOM- 19991216
LR  - 20190513
IS  - 0964-6906 (Print)
IS  - 0964-6906 (Linking)
VI  - 8
IP  - 11
DP  - 1999 Oct
TI  - Ectodysplasin is a collagenous trimeric type II membrane protein with a tumor
      necrosis factor-like domain and co-localizes with cytoskeletal structures at
      lateral and apical surfaces of cells.
PG  - 2079-86
AB  - Anhidrotic ectodermal dysplasia (EDA) is a human genetic disorder of impaired
      ectodermal appendage development. The EDA gene encodes isoforms of a novel
      transmembrane protein, ectodysplasin. The sequence of the longest isoform
      includes an interrupted collagenous domain of 19 Gly-X-Y repeats and a motif
      conserved in the tumor necrosis factor (TNF)-related ligand family. In order to
      understand better the function of the ectodysplasin protein molecule and its
      domains, we have studied the processing and localization of wild-type and mutated
      isoforms in transfected human fetal kidney 293 and monkey kidney COS-1 cells.
      Similar to other members of collagenous membrane proteins and members of
      TNF-related ligands, ectodysplasin is a type II membrane protein and it forms
      trimers. The membrane localization of ectodysplasin is asymmetrical: it is found 
      on the apical and lateral surfaces of the cells where it co-localizes with
      cytoskeletal structures. The TNF-like motif and cysteines found near the
      C-terminus are necessary for correct transport to the cell membrane, but the
      intracellular and collagenous domains are not required for the localization
      pattern. Our results suggest that ectodysplasin is a new member in the
      TNF-related ligand family involved in the early epithelial-mesenchymal
      interaction that regulates ectodermal appendage formation.
FAU - Ezer, S
AU  - Ezer S
AD  - Department of Medical Genetics, Haartman Institute, National Institute of Aging, 
      Baltimore, MD 21224, USA.
FAU - Bayes, M
AU  - Bayes M
FAU - Elomaa, O
AU  - Elomaa O
FAU - Schlessinger, D
AU  - Schlessinger D
FAU - Kere, J
AU  - Kere J
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Hum Mol Genet
JT  - Human molecular genetics
JID - 9208958
RN  - 0 (EDA protein, human)
RN  - 0 (Ectodysplasins)
RN  - 0 (Ligands)
RN  - 0 (Membrane Proteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Polarity
MH  - Collagen/chemistry
MH  - Cytoskeleton/*chemistry
MH  - Ectodermal Dysplasia/*genetics
MH  - Ectodysplasins
MH  - Humans
MH  - Ligands
MH  - Membrane Proteins/analysis/*chemistry/classification/genetics
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Protein Isoforms/*chemistry
MH  - *Protein Structure, Tertiary
MH  - Rats
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Subcellular Fractions/chemistry
MH  - Transfection
MH  - Tumor Necrosis Factor-alpha/metabolism
EDAT- 1999/09/15 00:00
MHDA- 1999/09/15 00:01
CRDT- 1999/09/15 00:00
PHST- 1999/09/15 00:00 [pubmed]
PHST- 1999/09/15 00:01 [medline]
PHST- 1999/09/15 00:00 [entrez]
AID - ddc233 [pii]
AID - 10.1093/hmg/8.11.2079 [doi]
PST - ppublish
SO  - Hum Mol Genet. 1999 Oct;8(11):2079-86. doi: 10.1093/hmg/8.11.2079.