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J Biol Chem, Vol. 273, Issue 18, 10811-10814, May 1, 1998
From the Howard Hughes Medical Institute, Cardiovascular Division,
Children's Hospital, Harvard Medical School, Boston, Massachusetts
02115
Since its cloning and tentative identification as
a chloride channel, the function of the pICln protein has been debated. Although there is no consensus regarding the specific function of
pICln, it was suggested to play a role, directly or indirectly, in the
function of a swelling-induced chloride conductance. Previously, the
protein was shown to exist in several discrete protein complexes. To
determine the function of the protein, we have begun the systematic identification of all proteins to which it binds. Here we show that
four proteins firmly bind to pICln and identify the 72-kDa pICln-binding protein by affinity purification and peptide
microsequencing. The interaction between this protein and pICln was
verified several ways, including the extraction of several pICln clones
from a cDNA library using the 72-kDa protein as a bait in a yeast
two-hybrid screen. The protein is homologous to the yeast Skb1 protein.
Skb1 interacts with Shk1, a homolog of the
p21Cdc42/Rac-activated protein kinases (PAKs). The
known involvement of PAKs in cytoskeletal rearrangement suggests that
pICln may be linked to a system regulating cell morphology.
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