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Blood, Vol. 92 No. 4 (August 15), 1998:
pp. 1442-1447
The 30-kD Domain of Protein 4.1 Mediates Its Binding to the Carboxyl
Terminus of pICln, a Protein Involved in Cellular Volume Regulation
Chieh-Ju C. Tang and
Tang K. Tang
From the Institute of Biomedical Sciences, Academia Sinica, Taipei,
Taiwan, Republic of China.
Erythrocyte protein 4.1 (P4.1) is an 80-kD cytoskeletal protein that
is important for the maintenance of the structural integrity and
flexibility of the red blood cell membrane. Limited chymotryptic digestion of erythroid P4.1 yields 4 structural domains corresponding to the 30-, 16-, 10-, and 22/24-kD domains. Using a yeast two-hybrid system, we isolated cDNA clones encoding pICln that specifically interacts with the 30-kD domain of P4.1. In this report, we show that
the carboxyl-terminus (amino acid residues 103-237) of pICln binds to
the 30-kD domain of P4.1 in a yeast two-hybrid system. The direct
association between the 30-kD domain of P4.1 and pICln was further
confirmed by the following findings: (1) the
S35-methione-labeled pICln specifically bound to both
GST/P4.1-80 (80 kD) and GST/P4.1-30 (30 kD) fusion proteins, but not to
the proteins that lack the 30-kD domain; (2) coimmunoprecipitation analysis of the cell extracts from transfected SiHa cells showed that
pICln and P4.1 associate in transfected cells. It was reported that
pICln can form a complex with actin and may play a role involved in
cellular volume regulation. The direct association between P4.1 and
pICln suggests that pICln may link P4.1-bound cytoskeletal elements to
an unidentified volume-sensitive chloride channel.
© 1998 by The American Society of Hematology.
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