Structural decoding of netrin-4 reveals a regulatory function towards mature basement membranes.

Abstract:

:Netrins, a family of laminin-related molecules, have been proposed to act as guidance cues either during nervous system development or the establishment of the vascular system. This was clearly demonstrated for netrin-1 via its interaction with the receptors DCC and UNC5s. However, mainly based on shared homologies with netrin-1, netrin-4 was also proposed to play a role in neuronal outgrowth and developmental/pathological angiogenesis via interactions with netrin-1 receptors. Here, we present the high-resolution structure of netrin-4, which shows unique features in comparison with netrin-1, and show that it does not bind directly to any of the known netrin-1 receptors. We show that netrin-4 disrupts laminin networks and basement membranes (BMs) through high-affinity binding to the laminin γ1 chain. We hypothesize that this laminin-related function is essential for the previously described effects on axon growth promotion and angiogenesis. Our study unveils netrin-4 as a non-enzymatic extracellular matrix protein actively disrupting pre-existing BMs.

journal_name

Nat Commun

journal_title

Nature communications

authors

Reuten R,Patel TR,McDougall M,Rama N,Nikodemus D,Gibert B,Delcros JG,Prein C,Meier M,Metzger S,Zhou Z,Kaltenberg J,McKee KK,Bald T,Tüting T,Zigrino P,Djonov V,Bloch W,Clausen-Schaumann H,Poschl E,Yurchenco PD,Eh

doi

10.1038/ncomms13515

subject

Has Abstract

pub_date

2016-11-30 00:00:00

pages

13515

issn

2041-1723

pii

ncomms13515

journal_volume

7

pub_type

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