V and C domains of Netrin-1 interact with the HBS of LIPG. Article Swipe
Ying Wang (11406)
,
Kazuhisa Murai (22881412)
,
Atsuya Ishida (8879114)
,
Narumi Kawasaki (22881415)
,
Kazuyuki Kuroki (10098666)
,
Ying-Yi Li (112692)
,
Yuga Sato (22881418)
,
Yutaro Miura (17026974)
,
Kureha Takara (22881421)
,
Lianghao Kong (22881424)
,
Tetsuro Shimakami (468623)
,
Kouki Nio (4530718)
,
Yuichiro Higuchi (498352)
,
Hiroshi Suemizu (278596)
,
Satoru Ito (283410)
,
Hiroshi Yanagawa (14718)
,
Shuichi Kaneko (156576)
,
Taro Yamashita (237137)
,
Masao Honda (156573)
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1371/journal.ppat.1013776.g003
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1371/journal.ppat.1013776.g003
A and B: Schematic representation of the heparin/heparan sulfate-binding sites of Netrin-1 and the substituted amino acid mutations. C: Diagram of wild-type LIPG and cleaved NTD and CTD, with or without deletion of the heparin-binding motif. D and E: HepG2 cells were co-transfected with a series of truncated forms of LIPG-HA and wild-type Netrin-1 V domain (V-Flag) (D) or heparin/heparan sulfate-binding site mutant V domain (V mut-V5) (E) plasmids. The cells were immunoprecipitated with α-HA antibody (for LIPG) and then detected with α-Flag antibody (for V) or α-V5 antibody (for V mut). F and G: HepG2 cells were co-transfected with a series of truncated forms of LIPG-HA and wild-type Netrin-1 C domain (C-Flag) (F) or heparin/heparan sulfate-binding site mutant C domain (C mut-V5) (G) plasmids. Cells were immunoprecipitated with α-HA antibody (for LIPG) and then detected with α-Flag antibody (for C) or α-V5 antibody (for C mut). H: A model of the Netrin-1 V domain interacting with LIPG. The Netrin-1 V domain interacts with the NTD heparin-binding motif of LIPG, while the heparin/heparan sulfate-binding site mutant V domain loses this ability. I: A model of the Netrin-1 C domain interacting with LIPG. The Netrin-1 C domain interacts with all domains of LIPG, while the heparin/heparan sulfate-binding site mutant C domain loses its affinity for the CTD heparin-binding motif of LIPG, but retains its affinity for the other domains. J: Dox-inducible full-length LIPG-HA-expressing HepG2-NTCP-YFP cells were co-transfected with full-length wild-type Netrin-1-Flag, mutant Netrin-1-V5 with heparin/heparan sulfate-binding site mutation in the V domain, and pcDNA3.1(+) empty plasmids (for a total of 4,250 ng plasmid per sample). The cells were incubated with 25 ng/mL Dox to induce LIPG expression. At 48 h after transfection, the cells were immunoprecipitated with α-HA antibody (for LIPG) and then detected with α-HA antibody (for LIPG), α-Flag antibody (for wild-type Netrin-1), or α-V5 antibody (for Netrin-1 with mutation in the V domain). K: Dox-inducible full-length LIPG-HA-expressing HepG2-NTCP-YFP cells were co-transfected with full-length wild-type Netrin-1-Flag, mutant Netrin-1-V5 with heparin/heparan sulfate-binding site mutation in the C domain, and pcDNA3.1(+) empty plasmids (for a total of 4,250 ng plasmid per sample). The cells were incubated with 25 ng/mL Dox to induce LIPG expression. At 48 h after transfection, the cells were immunoprecipitated with α-HA antibody (for LIPG) and then detected with α-HA antibody (for LIPG), α-Flag antibody (for wild-type Netrin-1), or α-V5 antibody (for Netrin-1 with mutation in the C domain).
Related Topics
Concepts
Mutant
Molecular biology
Immunoglobulin domain
Antibody
Chemistry
Peptide sequence
Mutation
Biology
Amino acid
Single-domain antibody
Immunoprecipitation
C2 domain
C-terminus
Domain (mathematical analysis)
Plasmid
Transfection
Binding site
Cell biology
Protein structure
Recombinant DNA
Protein domain
EGF-like domain
Structural motif
HEK 293 cells
Mutant protein
Binding domain
Mutagenesis
N-terminus
Metadata
- Type
- other
- OA Status
- green
- OpenAlex ID
- https://openalex.org/W7116085460
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W7116085460Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1371/journal.ppat.1013776.g003Digital Object Identifier
- Title
-
V and C domains of Netrin-1 interact with the HBS of LIPG.Work title
- Type
-
otherOpenAlex work type
- Publication year
-
2025Year of publication
- Publication date
-
2025-12-17Full publication date if available
- Authors
-
Ying Wang (11406), Kazuhisa Murai (22881412), Atsuya Ishida (8879114), Narumi Kawasaki (22881415), Kazuyuki Kuroki (10098666), Ying-Yi Li (112692), Yuga Sato (22881418), Yutaro Miura (17026974), Kureha Takara (22881421), Lianghao Kong (22881424), Tetsuro Shimakami (468623), Kouki Nio (4530718), Yuichiro Higuchi (498352), Hiroshi Suemizu (278596), Satoru Ito (283410), Hiroshi Yanagawa (14718), Shuichi Kaneko (156576), Taro Yamashita (237137), Masao Honda (156573)List of authors in order
- Open access
-
YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- Concepts
-
Mutant, Molecular biology, Immunoglobulin domain, Antibody, Chemistry, Peptide sequence, Mutation, Biology, Amino acid, Single-domain antibody, Immunoprecipitation, C2 domain, C-terminus, Domain (mathematical analysis), Plasmid, Transfection, Binding site, Cell biology, Protein structure, Recombinant DNA, Protein domain, EGF-like domain, Structural motif, HEK 293 cells, Mutant protein, Binding domain, Mutagenesis, N-terminusTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
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| best_oa_location.source.display_name | OPAL (Open@LaTrobe) (La Trobe University) |
| best_oa_location.source.host_organization | https://openalex.org/I196829312 |
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| best_oa_location.source.host_organization_lineage | https://openalex.org/I196829312 |
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| best_oa_location.pdf_url | |
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| best_oa_location.raw_type | Figure |
| best_oa_location.license_id | https://openalex.org/licenses/cc-by |
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| primary_location.id | pmh:oai:figshare.com:article/30905578 |
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| primary_location.source.host_organization_lineage | https://openalex.org/I196829312 |
| primary_location.license | cc-by |
| primary_location.pdf_url | |
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| publication_date | 2025-12-17 |
| publication_year | 2025 |
| referenced_works_count | 0 |
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