Protein kinase C zeta pseudosubstrate
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Protein kinase C zeta pseudosubstrate

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It is a protein kinase C inhibitor (PKC)ζ. It Consists of amino acids 113-129 PKC ζ pseudosubstrate domains connected by a disulfide bridge to the cell permeabilisation Antennapedia domain vector peptide.

Category
Peptide Inhibitors
Catalog number
BAT-009143
Molecular Formula
C208H336N74O44S3
Molecular Weight
4673.59
IUPAC Name
(2S)-6-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S,3S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2R)-2-amino-3-[[(2R)-2-amino-3-[[(2S)-1-[[(2S,3S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(1S)-3-amino-1-carboxy-3-oxopropyl]amino]-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-oxopropyl]disulfanyl]propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-phenylpropanoyl]amino]-5-oxopentanoyl]amino]-4-oxobutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylsulfanylbutanoyl]amino]hexanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]hexanoyl]amino]hexanoic acid
Synonyms
PKC ζ pseudosubstrate; H-Cys(1)-Ser-Ile-Tyr-Arg-Arg-Gly-Ala-Arg-Arg-Trp-Arg-Lys-Leu-Tyr-Arg-Ala-Asn-OH.H-Cys(1)-Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys-OH; L-cysteinyl-L-seryl-L-isoleucyl-L-tyrosyl-L-arginyl-L-arginyl-glycyl-L-alanyl-L-arginyl-L-arginyl-L-tryptophyl-L-arginyl-L-lysyl-L-leucyl-L-tyrosyl-L-arginyl-L-alanyl-L-asparagine (1->1')-disulfide compound with L-cysteinyl-L-arginyl-L-glutaminyl-L-isoleucyl-L-lysyl-L-isoleucyl-L-tryptophyl-L-phenylalanyl-L-glutaminyl-L-asparagyl-L-arginyl-L-arginyl-L-methionyl-L-lysyl-L-tryptophyl-L-lysyl-L-lysine
Appearance
White Lyophilized Solid
Purity
>98%
Sequence
CRQIKIWFQNRRMKWKK CSIYRRGARRWRKLYRAN* (Modifications: Disulfide bridge between 1-1*)
Storage
Store at -20°C
Solubility
Soluble in Water (2 mg/mL)
InChI
InChI=1S/C208H336N74O44S3/c1-12-110(6)163(195(320)268-135(54-27-32-81-212)184(309)280-164(111(7)13-2)197(322)277-154(99-120-104-249-130-50-23-20-47-125(120)130)192(317)272-149(94-115-43-16-15-17-44-115)188(313)266-144(73-75-158(216)286)182(307)275-155(100-160(218)288)193(318)264-142(63-41-90-245-207(234)235)176(301)258-139(60-38-87-242-204(228)229)177(302)267-146(77-92-327-11)183(308)257-134(53-26-31-80-211)180(305)273-152(97-118-102-247-128-48-21-18-45-123(118)128)190(315)260-132(51-24-29-78-209)178(303)269-147(198(323)324)55-28-33-82-213)281-185(310)145(74-76-159(217)287)265-173(298)138(59-37-86-241-203(226)227)254-168(293)126(214)107-328-329-108-127(215)169(294)279-157(106-283)194(319)282-165(112(8)14-3)196(321)276-151(96-117-67-71-122(285)72-68-117)189(314)262-140(61-39-88-243-205(230)231)174(299)255-131(56-34-83-238-200(220)221)170(295)250-105-162(290)251-113(9)166(291)253-137(58-36-85-240-202(224)225)172(297)259-143(64-42-91-246-208(236)237)181(306)274-153(98-119-103-248-129-49-22-19-46-124(119)129)191(316)263-141(62-40-89-244-206(232)233)175(300)256-133(52-25-30-79-210)179(304)270-148(93-109(4)5)186(311)271-150(95-116-65-69-121(284)70-66-116)187(312)261-136(57-35-84-239-201(222)223)171(296)252-114(10)167(292)278-156(199(325)326)101-161(219)289/h15-23,43-50,65-72,102-104,109-114,126-127,131-157,163-165,247-249,283-285H,12-14,24-42,51-64,73-101,105-108,209-215H2,1-11H3,(H2,216,286)(H2,217,287)(H2,218,288)(H2,219,289)(H,250,295)(H,251,290)(H,252,296)(H,253,291)(H,254,293)(H,255,299)(H,256,300)(H,257,308)(H,258,301)(H,259,297)(H,260,315)(H,261,312)(H,262,314)(H,263,316)(H,264,318)(H,265,298)(H,266,313)(H,267,302)(H,268,320)(H,269,303)(H,270,304)(H,271,311)(H,272,317)(H,273,305)(H,274,306)(H,275,307)(H,276,321)(H,277,322)(H,278,292)(H,279,294)(H,280,309)(H,281,310)(H,282,319)(H,323,324)(H,325,326)(H4,220,221,238)(H4,222,223,239)(H4,224,225,240)(H4,226,227,241)(H4,228,229,242)(H4,230,231,243)(H4,232,233,244)(H4,234,235,245)(H4,236,237,246)/t110-,111-,112-,113-,114-,126-,127-,131-,132-,133-,134-,135-,136-,137-,138-,139-,140-,141-,142-,143-,144-,145-,146-,147-,148-,149-,150-,151-,152-,153-,154-,155-,156-,157-,163-,164-,165-/m0/s1
InChI Key
BQLVLLVGFUIFFK-OXSGATHOSA-N
Canonical SMILES
CCC(C)C(C(=O)NC(CCCCN)C(=O)NC(C(C)CC)C(=O)NC(CC1=CNC2=CC=CC=C21)C(=O)NC(CC3=CC=CC=C3)C(=O)NC(CCC(=O)N)C(=O)NC(CC(=O)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCSC)C(=O)NC(CCCCN)C(=O)NC(CC4=CNC5=CC=CC=C54)C(=O)NC(CCCCN)C(=O)NC(CCCCN)C(=O)O)NC(=O)C(CCC(=O)N)NC(=O)C(CCCNC(=N)N)NC(=O)C(CSSCC(C(=O)NC(CO)C(=O)NC(C(C)CC)C(=O)NC(CC6=CC=C(C=C6)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCNC(=N)N)C(=O)NCC(=O)NC(C)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC7=CNC8=CC=CC=C87)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCCN)C(=O)NC(CC(C)C)C(=O)NC(CC9=CC=C(C=C9)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(C)C(=O)NC(CC(=O)N)C(=O)O)N)N
1. Protein Kinase C (PKC)ζ Pseudosubstrate Inhibitor Peptide Promiscuously Binds PKC Family Isoforms and Disrupts Conventional PKC Targeting and Translocation
Amy S Bogard, Steven J Tavalin Mol Pharmacol. 2015 Oct;88(4):728-35. doi: 10.1124/mol.115.099457. Epub 2015 Jul 21.
PKMζ is generated via an alternative transcriptional start site in the atypical protein kinase C (PKC)ζ isoform, which removes N-terminal regulatory elements, including the inhibitory pseudosubstrate domain, consequently rendering the kinase constitutively active. Persistent PKMζ activity has been proposed as a molecular mechanism for the long-term maintenance of synaptic plasticity underlying some forms of memory. Many studies supporting a role for PKMζ in synaptic plasticity and memory have relied on the PKCζ pseudosubstrate-derived ζ-inhibitory peptide (ZIP). However, recent studies have demonstrated that ZIP-induced impairments to synaptic plasticity and memory occur even in the absence of PKCζ, suggesting that ZIP exerts its actions via additional cellular targets. In this study, we demonstrated that ZIP interacts with conventional and novel PKC, in addition to atypical PKC isoforms. Moreover, when brain abundance of each PKC isoform and affinity for ZIP are taken into account, the signaling capacity of ZIP-responsive pools of conventional and novel PKCs may match or exceed that for atypical PKCs. Pseudosubstrate-derived peptides, like ZIP, are thought to exert their cellular action primarily by inhibiting PKC catalytic activity; however, the ZIP-sensitive catalytic core of PKC is known to participate in the enzyme's subcellular targeting, suggesting an additional mode of ZIP action. Indeed, we have demonstrated that ZIP potently disrupts PKCα interaction with the PKC-targeting protein A-kinase anchoring protein (AKAP) 79 and interferes with ionomycin-induced translocation of conventional PKC to the plasma membrane. Thus, ZIP exhibits broad-spectrum action toward the PKC family of enzymes, and this action may contribute to its unique ability to impair memory.
2. Protein Kinase C (PKC)ζ Pseudosubstrate Inhibitor Peptide Promiscuously Binds PKC Family Isoforms and Disrupts Conventional PKC Targeting and Translocation
Amy S Bogard, Steven J Tavalin Mol Pharmacol. 2015 Oct;88(4):728-35. doi: 10.1124/mol.115.099457. Epub 2015 Jul 21.
PKMζ is generated via an alternative transcriptional start site in the atypical protein kinase C (PKC)ζ isoform, which removes N-terminal regulatory elements, including the inhibitory pseudosubstrate domain, consequently rendering the kinase constitutively active. Persistent PKMζ activity has been proposed as a molecular mechanism for the long-term maintenance of synaptic plasticity underlying some forms of memory. Many studies supporting a role for PKMζ in synaptic plasticity and memory have relied on the PKCζ pseudosubstrate-derived ζ-inhibitory peptide (ZIP). However, recent studies have demonstrated that ZIP-induced impairments to synaptic plasticity and memory occur even in the absence of PKCζ, suggesting that ZIP exerts its actions via additional cellular targets. In this study, we demonstrated that ZIP interacts with conventional and novel PKC, in addition to atypical PKC isoforms. Moreover, when brain abundance of each PKC isoform and affinity for ZIP are taken into account, the signaling capacity of ZIP-responsive pools of conventional and novel PKCs may match or exceed that for atypical PKCs. Pseudosubstrate-derived peptides, like ZIP, are thought to exert their cellular action primarily by inhibiting PKC catalytic activity; however, the ZIP-sensitive catalytic core of PKC is known to participate in the enzyme's subcellular targeting, suggesting an additional mode of ZIP action. Indeed, we have demonstrated that ZIP potently disrupts PKCα interaction with the PKC-targeting protein A-kinase anchoring protein (AKAP) 79 and interferes with ionomycin-induced translocation of conventional PKC to the plasma membrane. Thus, ZIP exhibits broad-spectrum action toward the PKC family of enzymes, and this action may contribute to its unique ability to impair memory.
3. The zeta isozyme of protein kinase C binds to tubulin through the pseudosubstrate domain
M García-Rocha, J Avila, J Lozano Exp Cell Res. 1997 Jan 10;230(1):1-8. doi: 10.1006/excr.1996.3364.
It has been suggested that the protein kinase C zeta (zeta PKC) isoform is involved in mitogenic signaling in Xenopus oocytes and mammalian cells. Thus, the characterization of potential regulatory molecules that bind to zeta PKC is of great interest. We report here the identification by affinity chromatography of tubulin as a zeta PKC-binding protein. Further immunofluorescence and microtubule copolymerization studies are consistent with this interaction. It is suggested that tubulin binds to zeta PKC through its pseudosubstrate domain. Furthermore, results demonstrate that treatment of cells with nocodazole, which disrupts microtubule structures, severely impairs the activity of native zeta PKC, stressing the potential functional relevance of zeta PKC binding to tubulin.
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