@article{
 title = {Use of altered specificity mutants to probe a specific protein-protein interaction in differentiation: The GATA-1:FOG complex},
 type = {article},
 year = {1999},
 pages = {219-228},
 volume = {3},
 id = {ed2ce0ef-2974-32de-ac4b-b652a7d61a3b},
 created = {2023-01-10T01:46:46.200Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:46:46.200Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {GATA-1 and FOG (Friend of GATA-1) are each essential for erythroid and megakaryocyte development. FOG, a zinc finger protein, interacts with the amino (N) finger of GATA-1 and cooperates with GATA-1 to promote differentiation. To determine whether this interaction is critical for GATA- 1 action, we selected GATA-1 mutants in yeast that fail to interact with FOG but retain normal DNA binding, as well a compensatory FOG mutant that restores interaction. These novel GATA-1 mutants do not promote erythroid differentiation of GATA-1- erythroid cells. Differentiation is rescued by the second-site FOG mutant. Thus, interaction of FOG with GATA-1 is essential for the function of GATA-1 in erythroid differentiation. These findings provide a paradigm for dissecting protein-protein associations involved in mammalian development.},
 bibtype = {article},
 author = {Crispino, J.D. and Lodish, M.B. and MacKay, J.P. and Orkin, S.H.},
 doi = {10.1016/S1097-2765(00)80312-3},
 journal = {Molecular Cell},
 number = {2}
}

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