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A novel ADP‐ribosylation like factor (ARL‐6), interacts with the protein‐conducting channel SEC61β subunit
Author(s) -
Ingley E.,
Williams J.H.,
Walker C.E.,
Tsai S.,
Colley S.,
Sayer M.S.,
Tilbrook P.A.,
Sarna M.,
Beaumont J.G.,
Klinken S.P.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01188-6
Subject(s) - immunoprecipitation , heterotrimeric g protein , protein subunit , g alpha subunit , biology , microbiology and biotechnology , g protein , cell culture , gene , signal transduction , genetics
We report here the isolation of a new member of the ADP‐ribosylation factor (ARF)‐like family (ARL‐6) present in the J2E erythroleukemic cell line, but not its myeloid variants. Consistent with this lineage‐restricted expression, ARL‐6 mRNA increased with erythropoietin‐induced maturation of J2E cells, and decreased with interleukin 6‐induced differentiation of M1 monoblastoid cells. In tissues, ARL‐6 mRNA was most abundant in brain and kidney. While ARL‐6 protein was predominantly cytosolic, its membrane association increased following exposure to GTP‐γS, like many members of the ARF/ARL family. Using the yeast two‐hybrid system, six molecules which interact with ARL‐6 were identified including SEC61β, a subunit of the heterotrimeric protein conducting channel SEC61p. Co‐immunoprecipitation of ARL‐6 confirmed a stable association between ARL‐6 and SEC61β in COS cells. These results demonstrate that ARL‐6, a novel member of the ADP‐ribosylation factor‐like family, interacts with the SEC61β subunit.