EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gClq domains and participates in multimerization

Citation
R. Doliana et al., EMI, a novel cysteine-rich domain of EMILINs and other extracellular proteins, interacts with the gClq domains and participates in multimerization, FEBS LETTER, 484(2), 2000, pp. 164-168
Citations number
22
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
484
Issue
2
Year of publication
2000
Pages
164 - 168
Database
ISI
SICI code
0014-5793(20001103)484:2<164:EANCDO>2.0.ZU;2-H
Abstract
The N-terminal cysteine-rich domain (EMI domain) of EMILIN-1 is a new prote in domain that is shared with two proteins (multimerin and EMILIN-2) and wi th four additional database entries. The ERI domains are always located at the N-terminus, have a common gene organization, and belong to proteins tha t are forming or are compatible with multimer formation. The potential role of the EMI domain in the assembly of EMILIN-1 was investigated by the two- hybrid system. No reporter gene activity was detected when EMI-1 was co-tra nsformed with the C-terminal gC1q-1 domain excluding a head-to-tail multime rization: conversely, a strong interaction was detected when the EMI-1 doma in was co-transformed with the gC1q-2 domain of EMILIN-2. (C) 2000 Federati on of European Biochemical Societies. Published by Elsevier Science B.V. Al l rights reserved.