Sequence analysis of Arabidopsis thaliana E/ANTH-domain-containing proteins:: membrane tethers of the clathrin-dependent vesicle budding machinery

被引:40
作者
Holstein, SEH [1 ]
Oliviusson, P [1 ]
机构
[1] Heidelberg Univ, Heidelberg Inst Plant Sci, D-69120 Heidelberg, Germany
关键词
ANTH domain; clathrin-mediated vesicle budding; endocytosis; ENTH domain; phospholipid; protein interaction; VHS domain;
D O I
10.1007/s00709-005-0105-7
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The epsin N-terminal homology (ENTH) domain is a conserved protein module present in cytosolic proteins which are required in clathrin-mediated vesicle budding processes. A highly similar, yet unique module is the AP180 N-terminal homology (ANTH) domain, which is present in a set of proteins that also support clathrin-dependent endocytosis. Both ENTH and ANTH (E/ANTH) domains bind to phospholipids and proteins, in order to support the nucleation of clathrin coats on the plasma membrane or the trans-Golgi-network membrane. Therefore, E/ANTH proteins might be considered as universal tethering components of the clathrin-mediated vesicle budding machinery. Since the E/ANTH protein family appears to be crucial in the first steps of clathrin-coated vesicle budding, we performed data base searches of the Arabidopsis thaliana genome. Sequence analysis revealed three proteins containing the ENTH signature motif and eight proteins containing the ANTH signature motif. Another six proteins were found that do not contain either motif but seem to have the same domain structure and might therefore be seen as VHS-domain-containing plant proteins. Functional analysis of plant E/ANTH proteins are rather scarce, since only one ANTH homolog from A. thaliana, At-AP180, has been characterized so far. At-AP180 displays conserved functions as a clathrin assembly protein and as an alpha-adaptin binding partner, and in addition shows features at the molecular level that seem to be plant-specific.
引用
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页码:13 / 21
页数:9
相关论文
共 57 条
[1]   The yeast epsin Ent1 is recruited to membranes through multiple independent interactions [J].
Aguilar, RC ;
Watson, HA ;
Wendland, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (12) :10737-10743
[2]   PURIFICATION AND PROPERTIES OF A NEW CLATHRIN ASSEMBLY PROTEIN [J].
AHLE, S ;
UNGEWICKELL, E .
EMBO JOURNAL, 1986, 5 (12) :3143-3149
[3]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[4]   The U-box protein family in plants [J].
Azevedo, C ;
Santos-Rosa, MJ ;
Shirasu, K .
TRENDS IN PLANT SCIENCE, 2001, 6 (08) :354-358
[5]   Identification and functional characterization of Arabidopsis AP180, a binding partner of plant αC-adaptin [J].
Barth, M ;
Holstein, SEH .
JOURNAL OF CELL SCIENCE, 2004, 117 (10) :2051-2062
[6]   Accessory protein recruitment motifs in clathrin-mediated endocytosis [J].
Brett, TJ ;
Traub, LM ;
Fremont, DH .
STRUCTURE, 2002, 10 (06) :797-809
[7]   Biological basket weaving: Formation and function of clathrin-coated vesicles [J].
Brodsky, FM ;
Chen, CY ;
Knuehl, C ;
Towler, MC ;
Wakeham, DE .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2001, 17 :517-568
[8]   Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis [J].
Chen, H ;
Fre, S ;
Slepnev, VI ;
Capua, MR ;
Takei, K ;
Butler, MH ;
Di Fiore, PP ;
De Camilli, P .
NATURE, 1998, 394 (6695) :793-797
[9]   Specific interaction between SNARES and epsin N-terminal homology (ENTH) domains of epsin-related proteins in trans-Golgi network to endosome transport [J].
Chidambaram, S ;
Müllers, N ;
Wiederhold, K ;
Haucke, V ;
von Mollard, GF .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (06) :4175-4179
[10]  
Cremona O, 2001, J CELL SCI, V114, P1041