FB2026_03 , released September 17, 2026
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Citation
De Camilli, P., Chen, H., Hyman, J., Panepucci, E., Bateman, A., Brunger, A.T. (2002). The ENTH domain.  FEBS Lett. 513(1): 11--18.
FlyBase ID
FBrf0149608
Publication Type
Review
Abstract
The epsin NH2-terminal homology (ENTH) domain is a membrane interacting module composed by a superhelix of alpha-helices. It is present at the NH2-terminus of proteins that often contain consensus sequences for binding to clathrin coat components and their accessory factors, and therefore function as endocytic adaptors. ENTH domain containing proteins have additional roles in signaling and actin regulation and may have yet other actions in the nucleus. The ENTH domain is structurally similar to the VHS domain. These domains define two families of adaptor proteins which function in membrane traffic and whose interaction with membranes is regulated, in part, by phosphoinositides.
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    FEBS Lett.
    Title
    FEBS Letters
    Publication Year
    1968-
    ISBN/ISSN
    0014-5793
    Data From Reference
    Genes (5)