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 Communjournal_title
Nature communicationsauthors
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,Ehdoi
10.1038/ncomms13515subject
Has Abstractpub_date
2016-11-30 00:00:00pages
13515issn
2041-1723pii
ncomms13515journal_volume
7pub_type
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