Citation

BibTex format

@article{McKee:2021:10.1016/j.matbio.2021.05.004,
author = {McKee, KK and Hohenester, E and Aleksandrova, M and Yurchenco, PD},
doi = {10.1016/j.matbio.2021.05.004},
journal = {Matrix Biology},
pages = {49--63},
title = {Organization of the laminin polymer node},
url = {http://dx.doi.org/10.1016/j.matbio.2021.05.004},
volume = {98},
year = {2021}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Laminin polymerization is a key step of basement membrane assembly that depends on the binding of α, β and γ N-terminal LN domains to form a polymer node. Nodal assembly can be divided into two steps consisting of β- and γ-LN dimerization followed by calcium-dependent addition of the α-LN domain. The assembly and structural organization of laminin-111 LN-LEa segments was examined by size-exclusion chromatography (SEC) and electron microscopy. Triskelion-like structures were observed in negatively-stained images of purified α1/β1/γ1 LN-LEa trimers. Image averaging of these revealed a heel-to-toe organization of the LN domains with angled outward projections of the LEa stem-like domains. A series of single-amino acid substitutions was introduced into the polymerization faces of the α1, β1 and γ1 LN domains followed by SEC analysis to distinguish between loss of β-γ mediated dimerization and loss of α-dependent trimerization (with intact β-γ dimers). Dimer-blocking mutations were confined to the γ1-toe and the β1-heel, whereas the trimer-only-blocking mutations mapped to the γ1-heel, β1-toe and the α1-toe and heel. Thus, in the polymer node the γ1-toe pairs with the β1-heel, the β1-toe pairs with the α1-heel, and the α1-toe pairs with the γ1-heel.
AU - McKee,KK
AU - Hohenester,E
AU - Aleksandrova,M
AU - Yurchenco,PD
DO - 10.1016/j.matbio.2021.05.004
EP - 63
PY - 2021///
SN - 0174-173X
SP - 49
TI - Organization of the laminin polymer node
T2 - Matrix Biology
UR - http://dx.doi.org/10.1016/j.matbio.2021.05.004
UR - https://www.sciencedirect.com/science/article/pii/S0945053X21000445?via%3Dihub
UR - http://hdl.handle.net/10044/1/89719
VL - 98
ER -