A protein transduction domain located at the NH2-terminus of human translationally controlled tumor protein for delivery of active molecules to cells

Kim, Moonhee; Kim, Miyoung; Kim, Hyo Young; Kim, Sol; Jung, Jae‐Hoon; Maeng, Jeehye; Chang, Jun; Lee, Kyunglim

doi:10.1016/j.biomaterials.2010.08.077

Cited by 32 publications

(39 citation statements)

References 33 publications

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“…A synthetic N19 peptide also did not affect the intracellular functions. Kim et al have shown that N10 of HRF can work as a protein translocation domain (PTD) when fused with some proteins at their N termini (60). Protein internalization by this PTD was characterized by the high dose requirement (8-32 μM) and slow kinetics compared with that of TAT, an HIV-encoded peptide (61).…”

Section: Figurementioning

confidence: 99%

Histamine-releasing factor has a proinflammatory role in mouse models of asthma and allergy

Kashiwakura¹,

Ando²,

Matsumoto³

et al. 2012

J. Clin. Invest.

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Section: Figurementioning

confidence: 99%

Histamine-releasing factor has a proinflammatory role in mouse models of asthma and allergy

Kashiwakura¹,

Ando²,

Matsumoto³

et al. 2012

J. Clin. Invest.

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“…In certain cases TCTP displays a non-cell autonomous function in animals, as in the case of the histamine release factor (HRF), which is noteworthy, given the absence of a signal peptide in these proteins (Kang et al, 2001 ). In fact, TCTP is secreted via a non-classical pathway, for which it requires a peptide transduction domain (Amzallag et al, 2004 ; Kim et al, 2011 ). Structurally, TCTP is related to small GTP-binding proteins, and some evidence supports the notion that this protein functions as a guanine nucleotide exchange factor, although through which exact pathway is yet to be determined (Hsu et al, 2007 ).…”

Section: Introductionmentioning

confidence: 99%

AtTCTP2, an Arabidopsis thaliana homolog of Translationally Controlled Tumor Protein, enhances in vitro plant regeneration

et al. 2015

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The Translationally Controlled Tumor Protein (TCTP) is a central regulator of cell proliferation and differentiation in animals, and probably also in plants. Arabidopsis harbors two TCTP genes, AtTCTP1 (At3g16640), which is an important mitotic regulator, and AtTCTP2 (At3g05540), which is considered a pseudogene. Nevertheless, we have obtained evidence suggesting that this gene is functional. Indeed, a T-DNA insertion mutant, SALK_045146, displays a lethal phenotype during early rosette stage. Also, both the AtTCTP2 promoter and structural gene are functional, and heterozygous plants show delayed development. AtTCTP1 cannot compensate for the loss of AtTCTP2, since the accumulation levels of the AtTCTP1 transcript are even higher in heterozygous plants than in wild-type plants. Leaf explants transformed with Agrobacterium rhizogenes harboring AtTCTP2, but not AtTCTP1, led to whole plant regeneration with a high frequency. Insertion of a sequence present in AtTCTP1 but absent in AtTCTP2 demonstrates that it suppresses the capacity for plant regeneration; also, this phenomenon is enhanced by the presence of TCTP (AtTCTP1 or 2) in the nuclei of root cells. This confirms that AtTCTP2 is not a pseudogene and suggests the involvement of certain TCTP isoforms in vegetative reproduction in some plant species.

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“…The amino acid residues 76–110, part of the helical domain of Pm Fortilin are contained within a Ca 2+ -binding domain, forming a helical domain between the H2-helix (residues 81–99) and the H3-helix (residues 106–122) producing an EF-hand structure (Figure 1). Importantly, a small section at the N-terminus (residues 1–10) contains protein transduction domains (PTDs), 1-MKVFKDMLTG-10, allowing for the delivery of active molecules into the cells through the lipid bilayer [35]–[37]. Pm Fortilin contains two signature patterns.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a Novel Binding Protein for Fortilin/TCTP — Component of a Defense Mechanism against Viral Infection in Penaeus monodon

et al. 2012

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The Fortilin (also known as TCTP) in Penaeus monodon (PmFortilin) and Fortilin Binding Protein 1 (FBP1) have recently been shown to interact and to offer protection against the widespread White Spot Syndrome Virus infection. However, the mechanism is yet unknown. We investigated this interaction in detail by a number of in silico and in vitro analyses, including prediction of a binding site between PmFortilin/FBP1 and docking simulations. The basis of the modeling analyses was well-conserved PmFortilin orthologs, containing a Ca2+-binding domain at residues 76–110 representing a section of the helical domain, the translationally controlled tumor protein signature 1 and 2 (TCTP_1, TCTP_2) at residues 45–55 and 123–145, respectively. We found the pairs Cys59 and Cys76 formed a disulfide bond in the C-terminus of FBP1, which is a common structural feature in many exported proteins and the “x–G–K–K” pattern of the amidation site at the end of the C-terminus. This coincided with our previous work, where we found the “x–P–P–x” patterns of an antiviral peptide also to be located in the C-terminus of FBP1. The combined bioinformatics and in vitro results indicate that FBP1 is a transmembrane protein and FBP1 interact with N-terminal region of PmFortilin.

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A protein transduction domain located at the NH2-terminus of human translationally controlled tumor protein for delivery of active molecules to cells

Cited by 32 publications

References 33 publications

Histamine-releasing factor has a proinflammatory role in mouse models of asthma and allergy

Histamine-releasing factor has a proinflammatory role in mouse models of asthma and allergy

AtTCTP2, an Arabidopsis thaliana homolog of Translationally Controlled Tumor Protein, enhances in vitro plant regeneration

Characterization of a Novel Binding Protein for Fortilin/TCTP — Component of a Defense Mechanism against Viral Infection in Penaeus monodon

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