Signaling from the secretory granule to the nucleus: Uhmk1 and PAM

ABSTRACT: Neurons and endocrine cells package peptides in secretory granules (large dense core vesicles; LDCVs) for storage and stimulated release. Studies of PAM, an essential secretory granule membrane enzyme, revealed a pathway that can relay information from secretory granules to the nucleus, resulting in alterations in gene expression. The cytosolic domain of PAM, a type 1 membrane enzyme essential for the production of amidated peptides, is basally phosphorylated by Uhmk1 and other Ser/Thr kinases. Proopiomelanocortin processing in AtT-20 corticotrope tumor cells was increased when Uhmk1 expression was reduced. Uhmk1 was concentrated in the nucleus, but cycled rapidly between nucleus and cytosol. Endoproteolytic cleavage of PAM releases a soluble cytosolic domain (CD) fragment that locali

ORGANISM(S): Mus musculus

SUBMITTER: Chitra Rajagopal 

PROVIDER: E-GEOD-22509 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress