Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.

A synthetic peptide, KKKKRFSFKKSFKLSGFSFKK, containing the phosphorylation sites of the acidic 80-87 kDa protein kinase C substrate was used to identify phosphopeptides in enzyme digests of this protein from mouse fibroblast C3H/10T1/2 cells. Stimulation of phosphorylation occurred, in vivo, with TP...

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প্রধান লেখক: Amess, B, Manjarrez-Hernandez, H, Howell, SA, Learmonth, M, Aitken, A
বিন্যাস: Journal article
ভাষা:English
প্রকাশিত: 1992
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author Amess, B
Manjarrez-Hernandez, H
Howell, SA
Learmonth, M
Aitken, A
author_facet Amess, B
Manjarrez-Hernandez, H
Howell, SA
Learmonth, M
Aitken, A
author_sort Amess, B
collection OXFORD
description A synthetic peptide, KKKKRFSFKKSFKLSGFSFKK, containing the phosphorylation sites of the acidic 80-87 kDa protein kinase C substrate was used to identify phosphopeptides in enzyme digests of this protein from mouse fibroblast C3H/10T1/2 cells. Stimulation of phosphorylation occurred, in vivo, with TPA at Ser7, Ser11 and Ser18, and, with two less potent phorbol esters, at Ser7 and Ser18. Okadaic acid effected a net phosphorylation of Ser7 and/or Ser11. Solid-phase sequencing showed that, in vitro, the order of initial rate of phosphorylation was Ser11 greater than Ser7 greater than Ser18, while Ser18 was preferentially phosphorylated when either Ser7 or Ser11 was occupied. No significant phosphorylation of Ser15 was detected.
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spelling oxford-uuid:fd00a783-ff39-4ea1-bf0c-02cd138e6b8b2022-03-27T13:25:28ZMultisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fd00a783-ff39-4ea1-bf0c-02cd138e6b8bEnglishSymplectic Elements at Oxford1992Amess, BManjarrez-Hernandez, HHowell, SALearmonth, MAitken, AA synthetic peptide, KKKKRFSFKKSFKLSGFSFKK, containing the phosphorylation sites of the acidic 80-87 kDa protein kinase C substrate was used to identify phosphopeptides in enzyme digests of this protein from mouse fibroblast C3H/10T1/2 cells. Stimulation of phosphorylation occurred, in vivo, with TPA at Ser7, Ser11 and Ser18, and, with two less potent phorbol esters, at Ser7 and Ser18. Okadaic acid effected a net phosphorylation of Ser7 and/or Ser11. Solid-phase sequencing showed that, in vitro, the order of initial rate of phosphorylation was Ser11 greater than Ser7 greater than Ser18, while Ser18 was preferentially phosphorylated when either Ser7 or Ser11 was occupied. No significant phosphorylation of Ser15 was detected.
spellingShingle Amess, B
Manjarrez-Hernandez, H
Howell, SA
Learmonth, M
Aitken, A
Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.
title Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.
title_full Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.
title_fullStr Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.
title_full_unstemmed Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.
title_short Multisite phosphorylation of the 80 kDa (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts. Quantitative analysis of individual sites by solid-phase microsequencing.
title_sort multisite phosphorylation of the 80 kda marcks protein kinase c substrate in c3h 10t1 2 fibroblasts quantitative analysis of individual sites by solid phase microsequencing
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