Smoothened

Source: Wikipedia, the free encyclopedia.
SMO
Available structures
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Ensembl
UniProt
RefSeq (mRNA)

NM_005631

NM_176996

RefSeq (protein)

NP_005622

NP_795970

Location (UCSC)Chr 7: 129.19 – 129.21 MbChr 6: 29.74 – 29.76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Smoothened is a

teratogen cyclopamine.[7] It also is the target of vismodegib, the first hedgehog pathway inhibitor to be approved by the U.S. Food and Drug Administration (FDA).[8]

Smoothened (Smo) is a key

agonists and antagonists, such as SAG and vismodegib
, can bind to and activate or inhibit Smo, how Ptc inhibits Smo endogenously remains a mystery in the field.

Currently, Smo is targeted and inhibited directly by a small-molecule drug, vismodegib, for the treatment of advanced basal cell cancer, however widespread resistance to this drug has become a prevalent issue.[12][13] Finding another method to target Smo activity in Hh-driven cancers would provide valuable information for novel therapeutics. Identifying these Ptc responsive sites on Smo will help solve a long-standing mystery in Hh signaling and suggest new therapeutic strategies to block Smo activity in Hh-driven cancers.

Function

Overview of signal transduction pathways involved in apoptosis.

Cellular localization plays an essential role in the function of SMO, which anchors to the cell membrane as a 7-pass transmembrane protein. Stimulation of the

primary cilium in vertebrates in a process that involves the exit of patched from the primary cilium, where it normally localizes in its unstimulated state.[14] Vertebrate SMO that is mutated in the domain required for ciliary localisation often cannot contribute to hedgehog pathway activation.[15] Conversely, SMO can become constitutively localized to the primary cilium and potentially activate pathway signaling constitutively as a result of a tryptophan to leucine mutation in the aforementioned domain.[16] SMO has been shown to move during patched stimulation from the plasma membrane near the primary cilium to the ciliary membrane itself via a lateral transport pathway along the membrane, as opposed to via directed transport by vesicles. The cAMP-PKA pathway is known to promote the lateral movement of SMO and hedgehog signal transduction in general.[17] In invertebrates like Drosophila, SMO does not organize at cilia and instead is generally translocated to the plasma membrane following hedgehog binding to patched.[18]

After cellular localization, SMO must additionally be activated by a distinct mechanism in order to stimulate hedgehog signal transduction, but that mechanism is unknown.[19] There is evidence for the existence of an unidentified endogenous ligand that binds SMO and activates it. It is believed that mutations in SMO can mimic the ligand-induced conformation of SMO and activate constitutive signal transduction.[18]

SMO plays a key role in transcriptional repression and activation by the zinc-finger transcription factor

Evc2, but these mechanisms are not fully understood.[18]

Endogenous activation

Sterol Binding Sites in Smo CRD and TMD

A leading hypothesis in the field is that Ptc regulates Smo by gating its access to cholesterol or a related sterol.[24] It has been proposed that cholesterol activates Smo, and subsequently Hh signaling, by entering the active site through a hydrophobic “oxysterol tunnel,” which can adopt open or closed conformations to allow for activation or inactivation of Smo, respectively, due to allowed sterol binding.[25][26] Shh would work by inhibiting Ptc, which would increase accessible cholesterol concentrations and allow for the activation of Smo and transmission of the Hh signal.[27] A recent crystal structure has identified two sterol binding sites in Smo, but which site is endogenously regulated by Ptc remains to be determined. The potential sites of regulation include the extracellular cysteine-rich domain (CRD) of Smo, as well as a site deep within the transmembrane domain (TMD).[28][29][30]

Due to the abundance of cholesterol in the plasma membrane (up to 50 mole %), it has also been proposed that Ptc regulates the activity of Smo by controlling cholesterol accessibility specifically within the membrane of the

primary cilia, which contains a less abundant, and therefore more readily regulated pool of accessible cholesterol.[28][31]

Typically, upon activation and release of inhibition by Ptc, Smo will relocate to the primary cilia and Ptc will diffuse out of the ciliary membrane.[32] Upon inactivation, Smo no longer becomes concentrated in the ciliary membrane, This hypothesis is supported by methods which can increase or deplete the accessible cholesterol pool, with a subsequent increase or decrease in Hh signaling. This accessible cholesterol pool has been shown to be distinct from the general plasma membrane cholesterol pool in being available for protein interaction and cell uptake. The ciliary membrane has also been shown to contain lower levels of accessible cholesterol due to sequestering of cholesterol by sphingomyelin. In addition to cholesterol’s role as a Hh pathway agonist, it has been shown that cholesterol levels within the ciliary membrane rapidly increase upon treatment with Shh only in the presence of Ptc, further suggesting Ptc regulation of accessible cholesterol as the mechanism behind Smo activation/inhibition.[27] Additionally, Molecular Dynamics simulations suggest that vismodegib inhibits Smo through a conformational change that prevents cholesterol from binding.[33] This suggests the hypothesis that Ptc functions by preventing Smo access to cholesterol, and upon Ptc inhibition by Shh, Smo gains access to cholesterol and is subsequently activated, transmitting the Hh signal.

Role in disease

SMO can function as an oncogene. Activating SMO mutations can lead to unregulated activation of the hedgehog pathway and serve as driving mutations for cancers such as medulloblastoma, basal-cell carcinoma, pancreatic cancer, and prostate cancer.[16][34] As such, SMO is an attractive cancer drug target, along with the many hedgehog pathway agonists and antagonists that are known to directly target SMO.[16]

Cholesterol is known to be crucial in regulating the overall hedgehog pathway, and congenital mutations in cholesterol synthesis pathways can inactivate SMO specifically, leading to developmental disorders.[35] For example, oxysterol 20(S)-OHC is known to activate vertebrate SMO by binding the cysteine rich domain near its extracellular amino-terminal region. In the context of cancer, 20(S)-OHC is the target of a proposed anti-cancer oxysterol binding inhibitor.[18]

Agonists

Antagonists

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000128602Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001761Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. PMID 17094938
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  8. ^ "Vismodegib, First Hedgehog Inhibitor, Approved for BCC Patients". OncLive. Retrieved 2017-05-26.
  9. PMID 31092502
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  36. ^ Patidegib

Further reading

External links