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J Biol Chem, Vol. 274, Issue 5, 2929-2937, January 29, 1999
From the Departments of Neuroscience and Physiology, The Johns
Hopkins University School of Medicine, Baltimore, Maryland 21205, the
The production and regulated secretion of
bioactive peptides require a series of lumenal enzymes to convert
inactive precursors into bioactive peptides plus several cytosolic
proteins to govern granule formation, maturation, translocation, and
exocytosis. Peptidylglycine
Kalirin, a Multifunctional PAM COOH-terminal Domain Interactor
Protein, Affects Cytoskeletal Organization and ACTH Secretion from
AtT-20 Cells
, Departments of Surgery and Physiology, The University of
Maryland Medical School, Baltimore, Maryland 21201, and the
§ Institute of Biomedicine, Department of Anatomy,
University of Helsinki, Helsinki, Finland 00014
-amidating monooxygenase (PAM), an
enzyme essential for biosynthesis of many peptides, is an integral
membrane protein with trafficking information in both its lumenal and
cytosolic domains. Kalirin, a PAM cytosolic domain interactor protein
with spectrin-like repeats and GDP/GTP exchange factor activity for Rac1, is expressed with PAM in neurons but is not expressed in the
anterior pituitary or AtT-20 corticotrope cells. Expression of Kalirin
alters the cytoskeletal organization of Chinese hamster ovary and
AtT-20 cells expressing membrane PAM. Expression of membrane PAM also
alters cytoskeletal organization, demonstrating the presence of
endogenous proteins that can mediate this effect. Significant amounts
of both PAM and Kalirin fractionate with cytoskeletal elements. Since
cytoskeletal organization is critical for exocytosis, constitutive-like
and regulated secretions were evaluated. Whereas the constitutive-like
secretion of adrenocorticotropic hormone (ACTH) is increased by
expression of membrane PAM, regulated secretion is eliminated.
Expression of Kalirin in AtT-20 cells expressing membrane PAM restores
stimulated secretion of ACTH. Thus, Kalirin or its homologue may be
essential for regulated secretion, and the PAM-Kalirin interaction may
coordinate intragranular with cytosolic events.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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