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Titolo:
Signaling mediated by the cytosolic domain of peptidylglycine alpha-amidating monooxygenase
Autore:
Alam, MR; Steveson, TC; Johnson, RC; Back, N; Abraham, B; Mains, RE; Eipper, BA;
Indirizzi:
Univ Connecticut, Ctr Hlth, Dept Neurosci, Farmington, CT 06030 USA Univ Connecticut Farmington CT USA 06030 urosci, Farmington, CT 06030 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 3, volume: 12, anno: 2001,
pagine: 629 - 644
SICI:
1059-1524(200103)12:3<629:SMBTCD>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
PEPTIDE-PROCESSING ENZYME; IMMATURE SECRETORY GRANULES; GDP/GTP EXCHANGE FACTOR; PITUITARY-TUMOR-CELLS; TRANS-GOLGI NETWORK; PRO-ACTH-ENDORPHIN; ATT-20 CELLS; ROUTING DETERMINANTS; NEUROENDOCRINE CELLS; INTRACELLULAR-TRANSPORT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Eipper, BA Univ Connecticut, Ctr Hlth, Dept Neurosci, Farmington, CT 06030USA Univ Connecticut Farmington CT USA 06030 mington, CT 06030 USA
Citazione:
M.R. Alam et al., "Signaling mediated by the cytosolic domain of peptidylglycine alpha-amidating monooxygenase", MOL BIOL CE, 12(3), 2001, pp. 629-644

Abstract

The luminal domains of membrane peptidylglycine ce-amidating monooxygenase(PAM) are essential for peptide a-amidation, and the cytosolic domain (CD)is essential for trafficking. Overexpression of membrane PAM in corticotrope tumor cells reorganizes the actin cytoskeleton, shifts endogenous adrenocorticotropic hormone (ACTH) from mature granules localized at the tips of processes to the TGN region, and blocks regulated secretion. PAM-CD interactor proteins include a protein kinase that phosphorylates PAM (P-CIP2) and Kalirin, a Rho family GDP/GTP exchange factor. We engineered a PAM protein unable to interact with either P-CIP2 or Kalirin (PAM-1/K919R), along with PAM proteins able to interact with Kalirin but not with P-CIP2. AtT-20 cells expressing PAM-1/K919R produce fully active membrane enzyme but still exhibit regulated secretion, with ACTH-containing granules localized to process tips. Immunoelectron microscopy demonstrates accumulation of PAM and ACTHin tubular structures at the trans side of the Golgi in AtT-20 cells expressing PAM-1 but not in AtT-20 cells expressing PAM-1/K919R. The ability of PAM to interact with P-CIP2 is critical to its ability to block exit from the Golgi and affect regulated secretion. Consistent with this, mutation of its P-CIP2 phosphorylation site alters the ability of PAM to affect regulated secretion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 07:15:16