HDAC10: Difference between revisions

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'''HDAC10''' or '''Histone Deacetylase 10''' is a [[protein]] that in humans is encoded by the HDAC10 [[gene]]. It is part of the [[histone deacetylase]] family, which plays a key role in the regulation of [[eukaryotic]] gene expression.  
{{Infobox protein
| name = Histone deacetylase 10
| symbol = HDAC10
| image = <!-- Image removed -->
| width =
| caption =
| HGNCid = 14066
| OMIM = 606071
| RefSeq = NM_032019
| UniProt = Q969S8
| ECnumber = 3.5.1.98
| chromosome = 22
| arm = q
| band = 13.31
}}
 
'''Histone deacetylase 10''' ('''HDAC10''') is an [[enzyme]] that in humans is encoded by the '''HDAC10''' [[gene]]. This enzyme is part of the [[histone deacetylase]] family, which plays a critical role in the regulation of [[gene expression]] by modifying the [[chromatin]] structure.


== Function ==
== Function ==
HDAC10 is involved in the removal of [[acetyl groups]] from [[lysine]] residues on [[histone]] proteins, leading to chromatin condensation and transcriptional repression. This process is essential for the regulation of [[gene expression]] and is implicated in various cellular processes, including [[cell cycle]] progression, [[differentiation]], and [[apoptosis]].


HDAC10, like other members of the histone deacetylase family, is involved in the deacetylation of [[lysine]] residues on the [[nucleosome]] core histones, which is an important factor in the regulation of [[transcription (genetics)|transcription]]. Deacetylation of histones is associated with transcriptional repression and, in general, histone deacetylases (including HDAC10) are associated with [[transcription factor|transcription co-repressors]].
== Clinical significance ==
Alterations in HDAC10 expression have been associated with several [[cancers]], including [[neuroblastoma]] and [[colorectal cancer]]. Inhibitors targeting HDAC10 are being explored as potential [[therapeutic agents]] in cancer treatment due to their ability to induce [[cell cycle arrest]] and [[apoptosis]] in cancer cells.


== Structure ==
== Structure ==
HDAC10 is characterized by a unique structure that includes a catalytic domain similar to other [[class IIb histone deacetylases]]. It also contains a second domain that is thought to be involved in substrate recognition and binding.


The HDAC10 protein has a structure that is similar to other members of the histone deacetylase family. It contains a [[catalytic domain]] at its C-terminus and a [[NLS (protein)|nuclear localization signal]] at its N-terminus. The catalytic domain is responsible for the deacetylase activity of the protein, while the nuclear localization signal directs the protein to the [[nucleus (cell)|nucleus]] where it can interact with histones and other proteins.
== Interactions ==
 
HDAC10 interacts with various [[protein]]s and [[transcription factors]], influencing their activity and stability. These interactions are crucial for its role in regulating [[gene expression]] and maintaining [[cellular homeostasis]].
== Clinical significance ==


Alterations in the function of HDAC10 have been associated with several types of [[cancer]], including [[lung cancer]], [[breast cancer]], and [[leukemia]]. In these cases, the activity of HDAC10 is often upregulated, leading to increased deacetylation of histones and repression of tumor suppressor genes. Inhibitors of HDAC10 are currently being investigated as potential [[cancer treatment|treatments for cancer]].
== Research ==
 
Ongoing research is focused on understanding the specific substrates and biological pathways regulated by HDAC10. This knowledge could lead to the development of more selective HDAC10 inhibitors with improved therapeutic profiles.
[[File:HDAC10.png|thumb|right|Structure of HDAC10]]


== See also ==
== See also ==
* [[Histone deacetylase]]
* [[Histone deacetylase]]
* [[Gene expression]]
* [[Gene expression]]
* [[Transcription (genetics)]]
* [[Chromatin]]
* [[Cancer therapy]]


== References ==
== References ==
{{Reflist}}
{{Reflist}}


[[Category:Genes]]
== External links ==
[[Category:Proteins]]
* [https://www.ncbi.nlm.nih.gov/gene/83933 HDAC10 gene - NCBI]
[[Category:Enzymes]]
* [https://www.uniprot.org/uniprot/Q969S8 HDAC10 protein - UniProt]
[[Category:Epigenetics]]
[[Category:Oncology]]


{{medicine-stub}}
[[Category:Human proteins]]
[[Category:EC 3.5.1]]
[[Category:Histone deacetylases]]
[[Category:Genes on human chromosome 22]]

Latest revision as of 20:43, 30 December 2024


Histone deacetylase 10 (HDAC10) is an enzyme that in humans is encoded by the HDAC10 gene. This enzyme is part of the histone deacetylase family, which plays a critical role in the regulation of gene expression by modifying the chromatin structure.

Function[edit]

HDAC10 is involved in the removal of acetyl groups from lysine residues on histone proteins, leading to chromatin condensation and transcriptional repression. This process is essential for the regulation of gene expression and is implicated in various cellular processes, including cell cycle progression, differentiation, and apoptosis.

Clinical significance[edit]

Alterations in HDAC10 expression have been associated with several cancers, including neuroblastoma and colorectal cancer. Inhibitors targeting HDAC10 are being explored as potential therapeutic agents in cancer treatment due to their ability to induce cell cycle arrest and apoptosis in cancer cells.

Structure[edit]

HDAC10 is characterized by a unique structure that includes a catalytic domain similar to other class IIb histone deacetylases. It also contains a second domain that is thought to be involved in substrate recognition and binding.

Interactions[edit]

HDAC10 interacts with various proteins and transcription factors, influencing their activity and stability. These interactions are crucial for its role in regulating gene expression and maintaining cellular homeostasis.

Research[edit]

Ongoing research is focused on understanding the specific substrates and biological pathways regulated by HDAC10. This knowledge could lead to the development of more selective HDAC10 inhibitors with improved therapeutic profiles.

See also[edit]

References[edit]

<references group="" responsive="1"></references>


External links[edit]