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Interactome of Ca2+-bound secretagogin in mouse embryonic (E13.5) pancreas

ABSTRACT: By using His6-tagged recombinant human secretagogin in the presence of Ca2+ (100 µM), we isolated its putative interacting partners from mouse embryonic (E13.5) pancreata and identified their amino acid sequences by mass spectrometry. Next to previously described interacting partners (participating in vesicle-mediated transport, cytoskeletal organization and members of chaperonin-containing complex), we found a substantial group of proteins involved in proteasomal catabolic process including 15 different subunits of the 26S proteasome. Our data support that secretagogin protects Pdx1 from proteasomal degradation to control a transcriptional program required for β cell specification.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Pancreas

SUBMITTER: Edit Szodorai

LAB HEAD: Univ. Prof. Dr. Tibor Harkany

PROVIDER: PXD009516 | Pride | 2018-06-13

REPOSITORIES: Pride

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Secretagogin protects Pdx1 from proteasomal degradation to control a transcriptional program required for β cell specification.

Malenczyk Katarzyna K Szodorai Edit E Schnell Robert R Lubec Gert G Szabó Gábor G Hökfelt Tomas T Harkany Tibor T

Molecular metabolism 20180605

<h4>Objective</h4>Specification of endocrine cell lineages in the developing pancreas relies on extrinsic signals from non-pancreatic tissues, which initiate a cell-autonomous sequence of transcription factor activation and repression switches. The steps in this pathway share reliance on activity-dependent Ca<sup>2+</sup> signals. However, the mechanisms by which phasic Ca<sup>2+</sup> surges become converted into a dynamic, cell-state-specific and physiologically meaningful code made up by tran ...[more]

PMID: 29910119

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