Biosynthetic processing and quaternary interactions of proprotein convertase SPC4 (PACE4) (Q24313532)

GOA release 2020-03-11

protein processing

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GOA release 2020-03-11

author name string

M Nagahama

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T Taniguchi

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E Hashimoto

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A Imamaki

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K Mori

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A Tsuji

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Y Matsuda

The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions

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language of work or name

English

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publication date

28 August 1998

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published in

FEBS Letters

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volume

434

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issue

1-2

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page(s)

155-9

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cites work

1 reference

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Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins

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Identification of a Second Human Subtilisin-Like Protease Gene in thefes/fpsRegion of Chromosome 15

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Identification of novel cDNAs encoding human kexin-like protease, PACE4 isoforms

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Functional analysis of human PACE4-A and PACE4-C isoforms: identification of a new PACE4-CS isoform

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A novel human PACE4 isoform, PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus

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The tissue distribution of mRNAs for the PACE4 isoforms, kexin-like processing protease: PACE4C and PACE4D mRNAs are major transcripts among PACE4 isoforms

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Developmental expression of a novel Kexin family protease, PACE4E, in the rat olfactory system

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SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis.

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Genomic Organization and Alternative Splicing of Human PACE4 (SPC4), Kexin-Like Processing Endoprotease

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PACE4: a subtilisin-like endoprotease with unique properties

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Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum

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Autoproteolytic activation of the mouse prohormone convertase mPC1.

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Biosynthesis, Distinct Post-translational Modifications, and Functional Characterization of Lymphoma Proprotein Convertase

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Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage

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Two activation states of the prohormone convertase PC1 in the secretory pathway

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Characterization of PC2, a mammalian Kex2 homologue, following expression of the cDNA in microinjected Xenopus oocytes

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7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway

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Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events

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7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity

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Distribution of the Kexin family proteases in pancreatic islets: PACE4C is specifically expressed in B cells of pancreatic islets

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Positional and additive effects of basic amino acids on processing of precursor proteins within the constitutive secretory pathway

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Mutational analysis of PC1 (SPC3) in PC12 cells. 66-kDa PC1 is fully functional.

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