PuSH - Publication Server of Helmholtz Zentrum München

Saarikangas, J.* ; Kourdougli, N.* ; Senju, Y.* ; Chazal, G.* ; Segerstrale, M.* ; Minkeviciene, R.* ; Kuurne, J.* ; Mattila, P.K.* ; Garrett, L. ; Hölter, S.M. ; Becker, L. ; Rácz, I.* ; Hans, W. ; Klopstock, T.* ; Wurst, W. ; Zimmer, A.* ; Fuchs, H. ; Gailus-Durner, V. ; Hrabě de Angelis, M. ; von Ossowski, L.* ; Taira, T.* ; Lappalainen, P.* ; Rivera, C.* ; Hotulainen, P.*

MIM-induced membrane bending promotes dendritic spine initiation.

Dev. Cell 33, 644-659 (2015)
Publ. Version/Full Text DOI
Open Access Green as soon as Postprint is submitted to ZB.
Proper morphogenesis of neuronal dendritic spines is essential for the formation of functional synaptic networks. However, it is not known how spines are initiated. Here, we identify the inverse-BAR (I-BAR) protein MIM/MTSS1 as a nucleator of dendritic spines. MIM accumulated to future spine initiation sites in a PIP2-dependent manner and deformed the plasma membrane outward into a proto-protrusion via its I-BAR domain. Unexpectedly, the initial protrusion formation did not involve actin polymerization. However, PIP2-dependent activation of Arp2/3-mediated actin assembly was required for protrusion elongation. Overexpression of MIM increased the density of dendritic protrusions and suppressed spine maturation. In contrast, MIM deficiency led to decreased density of dendritic protrusions and larger spine heads. Moreover, MIM-deficient mice displayed altered glutamatergic synaptic transmission and compatible behavioral defects. Collectively, our data identify an important morphogenetic pathway, which initiates spine protrusions by coupling phosphoinositide signaling, direct membrane bending, and actin assembly to ensure proper synaptogenesis.
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Keywords Missing-in-metastasis; F-bar Domain; Actin Cytoskeleton; Plasma-membrane; Irsp53; Morphogenesis; Plasticity; Proteins; Dynamics; Shape
ISSN (print) / ISBN 1534-5807
e-ISSN 1878-1551
Quellenangaben Volume: 33, Issue: 6, Pages: 644-659 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place Cambridge
Reviewing status Peer reviewed