Protein kinase C (PKC) isozyme-specific substrates and their design

Jeong Hun Kang, Riki Toita, Chan Woo Kim, Yoshiki Katayama

Research output: Contribution to journalReview article

31 Citations (Scopus)

Abstract

Protein kinase C (PKC), a phospholipid-dependent serine/threonine kinase, appears to be involved in the signal transduction response to many hormones and growth factors; there are 11 different PKC isozymes. Because PKC isozymes directly and/or indirectly participate in signal transduction pathways of normal and transformed cells through phosphorylation of target proteins, it is critical to understand the diversity of the intracellular signaling pathways regulated by each PKC isozyme. Thus, PKC isozyme-specific substrates are useful to understand the characterization of the intracellular signaling pathways for each PKC isozyme. Consensus sequences and sequence information obtained from PKC target proteins are very important to design PKC isozyme-specific peptide substrates. Moreover, computational prediction programs of phosphorylation sites using a library of peptide substrates aid in the fast design of PKC isozyme-specific peptide substrates. Although a large number of target proteins and synthetic peptides for PKCs are known, only two peptide substrates (peptide 422-426 of murine elongation factor-1α and Alphatomega peptide) have been reported as PKC isozyme-specific peptide substrates. This discussion will review the literature concerning these native and synthetic PKC isozyme-specific peptide substrates and their design.

Original languageEnglish
Pages (from-to)1662-1672
Number of pages11
JournalBiotechnology Advances
Volume30
Issue number6
DOIs
Publication statusPublished - Nov 1 2012

Fingerprint

Protein Kinase C
Isoenzymes
Proteins
Peptides
Substrates
Signal transduction
Phosphorylation
Signal Transduction
Peptide Elongation Factor 1
Peptide Library
Protein-Serine-Threonine Kinases
Hormones
Consensus Sequence
Phospholipids
Intercellular Signaling Peptides and Proteins
Elongation

All Science Journal Classification (ASJC) codes

  • Biotechnology

Cite this

Protein kinase C (PKC) isozyme-specific substrates and their design. / Kang, Jeong Hun; Toita, Riki; Kim, Chan Woo; Katayama, Yoshiki.

In: Biotechnology Advances, Vol. 30, No. 6, 01.11.2012, p. 1662-1672.

Research output: Contribution to journalReview article

Kang, Jeong Hun ; Toita, Riki ; Kim, Chan Woo ; Katayama, Yoshiki. / Protein kinase C (PKC) isozyme-specific substrates and their design. In: Biotechnology Advances. 2012 ; Vol. 30, No. 6. pp. 1662-1672.
@article{915a170d326a45e1aa051f90d6b123c9,
title = "Protein kinase C (PKC) isozyme-specific substrates and their design",
abstract = "Protein kinase C (PKC), a phospholipid-dependent serine/threonine kinase, appears to be involved in the signal transduction response to many hormones and growth factors; there are 11 different PKC isozymes. Because PKC isozymes directly and/or indirectly participate in signal transduction pathways of normal and transformed cells through phosphorylation of target proteins, it is critical to understand the diversity of the intracellular signaling pathways regulated by each PKC isozyme. Thus, PKC isozyme-specific substrates are useful to understand the characterization of the intracellular signaling pathways for each PKC isozyme. Consensus sequences and sequence information obtained from PKC target proteins are very important to design PKC isozyme-specific peptide substrates. Moreover, computational prediction programs of phosphorylation sites using a library of peptide substrates aid in the fast design of PKC isozyme-specific peptide substrates. Although a large number of target proteins and synthetic peptides for PKCs are known, only two peptide substrates (peptide 422-426 of murine elongation factor-1α and Alphatomega peptide) have been reported as PKC isozyme-specific peptide substrates. This discussion will review the literature concerning these native and synthetic PKC isozyme-specific peptide substrates and their design.",
author = "Kang, {Jeong Hun} and Riki Toita and Kim, {Chan Woo} and Yoshiki Katayama",
year = "2012",
month = "11",
day = "1",
doi = "10.1016/j.biotechadv.2012.07.004",
language = "English",
volume = "30",
pages = "1662--1672",
journal = "Biotechnology Advances",
issn = "0734-9750",
publisher = "Elsevier Inc.",
number = "6",

}

TY - JOUR

T1 - Protein kinase C (PKC) isozyme-specific substrates and their design

AU - Kang, Jeong Hun

AU - Toita, Riki

AU - Kim, Chan Woo

AU - Katayama, Yoshiki

PY - 2012/11/1

Y1 - 2012/11/1

N2 - Protein kinase C (PKC), a phospholipid-dependent serine/threonine kinase, appears to be involved in the signal transduction response to many hormones and growth factors; there are 11 different PKC isozymes. Because PKC isozymes directly and/or indirectly participate in signal transduction pathways of normal and transformed cells through phosphorylation of target proteins, it is critical to understand the diversity of the intracellular signaling pathways regulated by each PKC isozyme. Thus, PKC isozyme-specific substrates are useful to understand the characterization of the intracellular signaling pathways for each PKC isozyme. Consensus sequences and sequence information obtained from PKC target proteins are very important to design PKC isozyme-specific peptide substrates. Moreover, computational prediction programs of phosphorylation sites using a library of peptide substrates aid in the fast design of PKC isozyme-specific peptide substrates. Although a large number of target proteins and synthetic peptides for PKCs are known, only two peptide substrates (peptide 422-426 of murine elongation factor-1α and Alphatomega peptide) have been reported as PKC isozyme-specific peptide substrates. This discussion will review the literature concerning these native and synthetic PKC isozyme-specific peptide substrates and their design.

AB - Protein kinase C (PKC), a phospholipid-dependent serine/threonine kinase, appears to be involved in the signal transduction response to many hormones and growth factors; there are 11 different PKC isozymes. Because PKC isozymes directly and/or indirectly participate in signal transduction pathways of normal and transformed cells through phosphorylation of target proteins, it is critical to understand the diversity of the intracellular signaling pathways regulated by each PKC isozyme. Thus, PKC isozyme-specific substrates are useful to understand the characterization of the intracellular signaling pathways for each PKC isozyme. Consensus sequences and sequence information obtained from PKC target proteins are very important to design PKC isozyme-specific peptide substrates. Moreover, computational prediction programs of phosphorylation sites using a library of peptide substrates aid in the fast design of PKC isozyme-specific peptide substrates. Although a large number of target proteins and synthetic peptides for PKCs are known, only two peptide substrates (peptide 422-426 of murine elongation factor-1α and Alphatomega peptide) have been reported as PKC isozyme-specific peptide substrates. This discussion will review the literature concerning these native and synthetic PKC isozyme-specific peptide substrates and their design.

UR - http://www.scopus.com/inward/record.url?scp=84867705071&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84867705071&partnerID=8YFLogxK

U2 - 10.1016/j.biotechadv.2012.07.004

DO - 10.1016/j.biotechadv.2012.07.004

M3 - Review article

C2 - 22841933

AN - SCOPUS:84867705071

VL - 30

SP - 1662

EP - 1672

JO - Biotechnology Advances

JF - Biotechnology Advances

SN - 0734-9750

IS - 6

ER -