PT  - JOURNAL ARTICLE
AU  - Kendra L Taylor
AU  - Russell J Taylor
AU  - Karl E Richters
AU  - Brandon Huynh
AU  - Justin Carrington
AU  - Maeve E McDermott
AU  - Rebecca L Wilson
AU  - Erik W Dent
TI  - Opposing functions of F-BAR proteins in neuronal membrane protrusion, tubule formation, and neurite outgrowth
AID  - 10.26508/lsa.201800288
DP  - 2019 Jun 01
TA  - Life Science Alliance
PG  - e201800288
VI  - 2
IP  - 3
4099  - https://www.life-science-alliance.org/content/2/3/e201800288.short
4100  - https://www.life-science-alliance.org/content/2/3/e201800288.full
SO  - Life Sci. Alliance2019 Jun 01; 2
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.