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Multifaceted role of tensins in cancer

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53 days ago
Multifaceted role of tensins in cancer https://t.co/kegaxHt82I https://t.co/97v8nPGNcA
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Supplemental Information

Figure 1 - Structure of members of the Tensin family and phylogenetic tree

(A) Structure of members of the Tensin family. Tensin-1, Tensin-2 and Tensin-3 contain an ABD (actin binding domain), SH2 (Src homology 2) domain and PTB (phosphotyrosine binding domain). Tensin-2 has a conserved protein kinase C region 1 that is not present in other Tensins. TNS4 has a SH2 domain and PTB domain but lacks the ABD. Among all Tensins, Nuclear localization signal (NLS) and Nuclear export signal (NES) was identified in TNS4. (B) Molecular Phylogenetic analysis of tensins by Maximum Likelihood method

DOI: 10.7287/peerj.preprints.27990v1/supp-1

Figure 2 - Phylogenetic tree of tensin 4 in domestic mammals

Molecular Phylogenetic analysis of tensin 4 in domestic mammals by Maximum Likelihood method

DOI: 10.7287/peerj.preprints.27990v1/supp-2

Figure 3 - NLS Alignment in tensins

Alignment of NLS regions in the four tensins and highlighted conserved amino acid residues.

DOI: 10.7287/peerj.preprints.27990v1/supp-3

Figure 4 - Homology for the SH2 domain in the four tensins

Homology for the SH2 domain across the four tensins. High conservation of tyrosine (Y) residues is indicated by * and low conservavtion indicated by +.

DOI: 10.7287/peerj.preprints.27990v1/supp-4

Figure 5 - TNS3 and TNS4 upregulation

TNS3 and TNS4 upregulation following EGF stimulation in colorectal cancer.

DOI: 10.7287/peerj.preprints.27990v1/supp-5

Figure 6 - TNS1-DLC1 interaction

TNS1 interaction with DLC1 and effects on RhoA.

DOI: 10.7287/peerj.preprints.27990v1/supp-6

Figure 7 - TNS4-Beta-catenin interaction

Predicted interaction between the N-terminal part of TNS4 and a grove in the armadillo structure of Beta-catenin.

DOI: 10.7287/peerj.preprints.27990v1/supp-7

Figure 8 - Network of Beta-catenin and TNS4 interactors

Network of Beta-catenin and TNS4 interactors (thebiogrid.org). EGFR (circled in red) is a common interactor for both proteins.

DOI: 10.7287/peerj.preprints.27990v1/supp-8

Supplementary Figure 1

Tensins 1-4 homology alignment and highlighted domains. ABD - Actin-binding domain; PTP - Phosphatase Tensin type; C1 - Protein kinase C conserved region; C2 - tensin type domain, SH2 - Src homology region, PTB - phosphotyrosine binding region NLS - nuclear localization signal.

DOI: 10.7287/peerj.preprints.27990v1/supp-9

Table 1 - In vitro assays of TNS4 function and TNS4 expression in clinical samples

Summary of the reported functions of TNS4 in vitro and associations between TNS4 expression in clinical samples and patient outcomes in various types of cancerous and normal tissues.

DOI: 10.7287/peerj.preprints.27990v1/supp-10

Additional Information

Competing Interests

The authors declare that they have no competing interests.

Author Contributions

Abdulaziz Alfahed conceived and designed the experiments, performed the experiments, contributed reagents/materials/analysis tools, prepared figures and/or tables, authored or reviewed drafts of the paper, approved the final draft.

Teresa P Raposo conceived and designed the experiments, analyzed the data, contributed reagents/materials/analysis tools, prepared figures and/or tables, authored or reviewed drafts of the paper, approved the final draft.

Mohammad Ilyas conceived and designed the experiments, authored or reviewed drafts of the paper, approved the final draft.

Data Deposition

The following information was supplied regarding data availability:

Supplementary Figure 1 - Tensins 1-4 homology alignment and highlighted domains. ABD - Actin-binding domain; PTP - Phosphatase Tensin type; C1 - Protein kinase C conserved region; C2 - , SH2 - Src homology region, PTB - phosphotyrosine binding region, NLS - nuclear localization signal.

Funding

This work was supported by a grant (RA4852) attributed to the Nottingham Molecular Pathology Node by the Medical Research Council, United Kingdom. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.


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