RT Journal Article
SR Electronic
T1 Opposing functions of F-BAR proteins in neuronal membrane protrusion, tubule formation, and neurite outgrowth
JF Life Science Alliance
JO Life Sci. Alliance
FD Life Science Alliance LLC
SP e201800288
DO 10.26508/lsa.201800288
VO 2
IS 3
A1 Taylor, Kendra L
A1 Taylor, Russell J
A1 Richters, Karl E
A1 Huynh, Brandon
A1 Carrington, Justin
A1 McDermott, Maeve E
A1 Wilson, Rebecca L
A1 Dent, Erik W
YR 2019
UL http://www.life-science-alliance.org/content/2/3/e201800288.abstract
AB The F-BAR family of proteins play important roles in many cellular processes by regulating both membrane and actin dynamics. The CIP4 family of F-BAR proteins is widely recognized to function in endocytosis by elongating endocytosing vesicles. However, in primary cortical neurons, CIP4 concentrates at the tips of extending lamellipodia and filopodia and inhibits neurite outgrowth. Here, we report that the highly homologous CIP4 family member, FBP17, induces tubular structures in primary cortical neurons and results in precocious neurite formation. Through domain swapping and deletion experiments, we demonstrate that a novel polybasic region between the F-BAR and HR1 domains is required for membrane bending. Moreover, the presence of a poly-PxxP region in longer splice isoforms of CIP4 and FBP17 largely reverses the localization and function of these proteins. Thus, CIP4 and FBP17 function as an antagonistic pair to fine-tune membrane protrusion, endocytosis, and neurite formation during early neuronal development.