TY - JOUR
T1 - A role for epsin N-terminal homology/AP180 N-terminal homology (ENTH/ANTH) domains in tubulin binding
AU - Hussain, Natasha K.
AU - Yamabhai, Montarop
AU - Bhakar, Asha L.
AU - Metzler, Martina
AU - Ferguson, Stephen S.G.
AU - Hayden, Michael R.
AU - McPherson, Peter S.
AU - Kay, Brian K.
PY - 2003/8/1
Y1 - 2003/8/1
N2 - The epsin N-terminal homology (ENTH) domain is a protein module of ∼150 amino acids found at the N terminus of a variety of proteins identified in yeast, plants, nematode, frog, and mammals. ENTH domains comprise multiple α-helices folded upon each other to form a compact globular structure that has been implicated in interactions with lipids and proteins. In characterizing this evolutionarily conserved domain, we isolated and identified tubulin as an ENTH domain-binding partner. The interaction, which is direct and has a dissociation constant of ∼1 μM, was observed with ENTH domains of proteins present in various species. Tubulin is co-immunoprecipitated from rat brain extracts with the ENTH domain-containing proteins, epsins 1 and 2, and punctate epsin staining is observed along the microtubule cytoskeleton of dissociated cortical neurons. Consistent with a role in microtubule processes, the over-expression of epsin ENTH domain in PC12 cells stimulates neurite outgrowth. These data demonstrate an evolutionarily conserved property of ENTH domains to interact with tubulin and microtubules.
AB - The epsin N-terminal homology (ENTH) domain is a protein module of ∼150 amino acids found at the N terminus of a variety of proteins identified in yeast, plants, nematode, frog, and mammals. ENTH domains comprise multiple α-helices folded upon each other to form a compact globular structure that has been implicated in interactions with lipids and proteins. In characterizing this evolutionarily conserved domain, we isolated and identified tubulin as an ENTH domain-binding partner. The interaction, which is direct and has a dissociation constant of ∼1 μM, was observed with ENTH domains of proteins present in various species. Tubulin is co-immunoprecipitated from rat brain extracts with the ENTH domain-containing proteins, epsins 1 and 2, and punctate epsin staining is observed along the microtubule cytoskeleton of dissociated cortical neurons. Consistent with a role in microtubule processes, the over-expression of epsin ENTH domain in PC12 cells stimulates neurite outgrowth. These data demonstrate an evolutionarily conserved property of ENTH domains to interact with tubulin and microtubules.
UR - http://www.scopus.com/inward/record.url?scp=0042707888&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0042707888&partnerID=8YFLogxK
U2 - 10.1074/jbc.M300995200
DO - 10.1074/jbc.M300995200
M3 - Article
C2 - 12750376
AN - SCOPUS:0042707888
SN - 0021-9258
VL - 278
SP - 28823
EP - 28830
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 31
ER -