Abstract
A general aim of studies of signal transduction is to identify mediators of specific signals, order them into pathways, and understand the nature of interactions between individual components and how these interactions alter pathway behavior. Despite years of intensive study and its central importance to animal development and human health, our understanding of the Hedgehog (Hh) signaling pathway remains riddled with gaps, question marks, assumptions, and poorly understood connections. In particular, understanding how interactions between Hh and Patched (Ptc), a 12-pass integral membrane protein, lead to modulation of the function of Smoothened (Smo), a 7-pass integral membrane protein, has defied standard biochemical characterization. Recent structural and biochemical characterizations of Smoothened domains have begun to unlock this riddle, however, and lay the groundwork for improved cancer therapies.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3500-3507 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 290 |
| Issue number | 6 |
| DOIs | |
| State | Published - Feb 6 2015 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
Smoothened goes molecular : New pieces in the hedgehog signaling puzzle. / McCabe, Jacqueline M.; Leahy, Daniel J.
In: Journal of Biological Chemistry, Vol. 290, No. 6, 06.02.2015, p. 3500-3507.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Smoothened goes molecular
T2 - New pieces in the hedgehog signaling puzzle
AU - McCabe, Jacqueline M.
AU - Leahy, Daniel J.
PY - 2015/2/6
Y1 - 2015/2/6
N2 - A general aim of studies of signal transduction is to identify mediators of specific signals, order them into pathways, and understand the nature of interactions between individual components and how these interactions alter pathway behavior. Despite years of intensive study and its central importance to animal development and human health, our understanding of the Hedgehog (Hh) signaling pathway remains riddled with gaps, question marks, assumptions, and poorly understood connections. In particular, understanding how interactions between Hh and Patched (Ptc), a 12-pass integral membrane protein, lead to modulation of the function of Smoothened (Smo), a 7-pass integral membrane protein, has defied standard biochemical characterization. Recent structural and biochemical characterizations of Smoothened domains have begun to unlock this riddle, however, and lay the groundwork for improved cancer therapies.
AB - A general aim of studies of signal transduction is to identify mediators of specific signals, order them into pathways, and understand the nature of interactions between individual components and how these interactions alter pathway behavior. Despite years of intensive study and its central importance to animal development and human health, our understanding of the Hedgehog (Hh) signaling pathway remains riddled with gaps, question marks, assumptions, and poorly understood connections. In particular, understanding how interactions between Hh and Patched (Ptc), a 12-pass integral membrane protein, lead to modulation of the function of Smoothened (Smo), a 7-pass integral membrane protein, has defied standard biochemical characterization. Recent structural and biochemical characterizations of Smoothened domains have begun to unlock this riddle, however, and lay the groundwork for improved cancer therapies.
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U2 - 10.1074/jbc.R114.617936
DO - 10.1074/jbc.R114.617936
M3 - Article
C2 - 25519909
AN - SCOPUS:84922358758
VL - 290
SP - 3500
EP - 3507
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 6
ER -