Abstract
KCTD15 is a member of the K+ Channel Tetramerization Domain family, implicated in crucial physio-pathological processes. Recent evidences suggest that KCTD15 is an obesity-linked protein in humans and its Drosophila homologue is involved in food uptake. KCTD15 molecular mechanism in these processes is still unknown. To fill this gap, KCTD15 was biophysically characterized showing a folded, pentameric region endowed with a remarkable thermal stability. Notably, the C-terminal domain significantly contributes to the stabilization of the BTB N-terminal domain. The availability of large amount of stable recombinant protein also made possible a functional proteomic approach in 3T3-L1 cells to search for novel KCTD15 interactors. These investigations led to the discovery that GRP78 is a KCTD15 partner in all the adipogenesis phases. Our data clearly prove the physical interaction of the two proteins and also indicate that GRP78 plays an active role in the stabilization of KCTD15. Furthermore, the presence in Drosophila of a GRP78 homologue corroborates the physiological role played by the complex KCTD15-GRP78 in the adipogenesis process and indicates that it is evolutionarily conserved. Present results also suggest that KCTD15 may be a new target for obesity control.
| Original language | English |
|---|---|
| Pages (from-to) | 469-475 |
| Number of pages | 7 |
| Journal | International Journal of Biological Macromolecules |
| Volume | 115 |
| DOIs | |
| Publication status | Published - Aug 1 2018 |
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Keywords
- Adipogenesis
- Interactors
- KCTD family
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology
Cite this
The essential player in adipogenesis GRP78 is a novel KCTD15 interactor. / Smaldone, Giovanni; Pirone, Luciano; Capolupo, Angela; Vitagliano, Luigi; Monti, Maria Chiara; Di Gaetano, Sonia; Pedone, Emilia.
In: International Journal of Biological Macromolecules, Vol. 115, 01.08.2018, p. 469-475.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The essential player in adipogenesis GRP78 is a novel KCTD15 interactor
AU - Smaldone, Giovanni
AU - Pirone, Luciano
AU - Capolupo, Angela
AU - Vitagliano, Luigi
AU - Monti, Maria Chiara
AU - Di Gaetano, Sonia
AU - Pedone, Emilia
PY - 2018/8/1
Y1 - 2018/8/1
N2 - KCTD15 is a member of the K+ Channel Tetramerization Domain family, implicated in crucial physio-pathological processes. Recent evidences suggest that KCTD15 is an obesity-linked protein in humans and its Drosophila homologue is involved in food uptake. KCTD15 molecular mechanism in these processes is still unknown. To fill this gap, KCTD15 was biophysically characterized showing a folded, pentameric region endowed with a remarkable thermal stability. Notably, the C-terminal domain significantly contributes to the stabilization of the BTB N-terminal domain. The availability of large amount of stable recombinant protein also made possible a functional proteomic approach in 3T3-L1 cells to search for novel KCTD15 interactors. These investigations led to the discovery that GRP78 is a KCTD15 partner in all the adipogenesis phases. Our data clearly prove the physical interaction of the two proteins and also indicate that GRP78 plays an active role in the stabilization of KCTD15. Furthermore, the presence in Drosophila of a GRP78 homologue corroborates the physiological role played by the complex KCTD15-GRP78 in the adipogenesis process and indicates that it is evolutionarily conserved. Present results also suggest that KCTD15 may be a new target for obesity control.
AB - KCTD15 is a member of the K+ Channel Tetramerization Domain family, implicated in crucial physio-pathological processes. Recent evidences suggest that KCTD15 is an obesity-linked protein in humans and its Drosophila homologue is involved in food uptake. KCTD15 molecular mechanism in these processes is still unknown. To fill this gap, KCTD15 was biophysically characterized showing a folded, pentameric region endowed with a remarkable thermal stability. Notably, the C-terminal domain significantly contributes to the stabilization of the BTB N-terminal domain. The availability of large amount of stable recombinant protein also made possible a functional proteomic approach in 3T3-L1 cells to search for novel KCTD15 interactors. These investigations led to the discovery that GRP78 is a KCTD15 partner in all the adipogenesis phases. Our data clearly prove the physical interaction of the two proteins and also indicate that GRP78 plays an active role in the stabilization of KCTD15. Furthermore, the presence in Drosophila of a GRP78 homologue corroborates the physiological role played by the complex KCTD15-GRP78 in the adipogenesis process and indicates that it is evolutionarily conserved. Present results also suggest that KCTD15 may be a new target for obesity control.
KW - Adipogenesis
KW - Interactors
KW - KCTD family
UR - http://www.scopus.com/inward/record.url?scp=85046012193&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85046012193&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2018.04.078
DO - 10.1016/j.ijbiomac.2018.04.078
M3 - Article
C2 - 29665387
AN - SCOPUS:85046012193
VL - 115
SP - 469
EP - 475
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
ER -