PPP6R3

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The PPP6R3 gene (also termed C11orf23, PP6R3, SAP190, SAPL, SAPLa, and SAPS3 [1] ) is located at band 13.2 on the long (or "q") arm of chromosome 11 and is expressed in all tissues tested. [2] It encodes protein phosphatase 6 regulatory subunit 3 (PP6RS3). [3] Also termed serine/threonine-protein phosphatase 6 regulatory subunit 3, PP6RS3 is the function-regulating subunit of protein phosphatase 6 (PPP6C). [4] PPP6C is a component of a signaling pathway that regulates various cell functions including cell division, the repair of damaged DNA, inflammatory responses, [5] messenger mRNA splicing, and the stability of chromosomes. [6]

Two cases of nodular fasciitis have malignant tumors in which the neoplastic cells expressed a PPP6R3 gene merged to the USP6 (i.e. ubiquitin carboxyl-terminal hydrolase 6) gene to form an USP-PPP6R3 fusion gene. In both of these cases, the USP-PPP6R3 fusion genes was considered to contribute to these tumors malignancy. [3] [6] [7]

Related Research Articles

Nodular fasciitis Medical condition

Nodular fasciitis (NF) is a benign, soft tissue tumor composed of myofibroblasts that typically occurs in subcutaneous tissue, fascia, and/or muscles. The literature sometimes titles rare NF variants according to their tissue locations. The most frequently used and important of these are: cranial fasciitis and intravascular fasciitis. In 2020, the World Health Organization classified nodular fasciitis as in the category of benign fibroblastic/myofibroblastic tumors. NF is the most common of the benign fibroblastic proliferative tumors of soft tissue and exceeds in frequency any other tumor or tumor-like lesion in this group of tumors.

PPP2R1A

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform is an enzyme that in humans is encoded by the PPP2R1A gene. In the plant Arabidopsis thaliana a similar enzyme is encoded by the RCN1 gene (At1g25490).

PPP5C

Serine/threonine-protein phosphatase 5 is an enzyme that in humans is encoded by the PPP5C gene.

PPP2R5A

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform is an enzyme that in humans is encoded by the PPP2R5A gene.

PPP1CB

Serine/threonine-protein phosphatase PP1-beta catalytic subunit is an enzyme that in humans is encoded by the PPP1CB gene.

PPP2R5C

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform is an enzyme that in humans is encoded by the PPP2R5C gene.

PPP2R1B

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform is an enzyme that in humans is encoded by the PPP2R1B gene.

PPP2R5D

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform is an enzyme that in humans is encoded by the PPP2R5D gene. Mutations in PPP2R5D cause Jordan's Syndrome.

PPP2R2C

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform is an enzyme that in humans is encoded by the PPP2R2C gene.

PPP2R5B

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform is an enzyme that in humans is encoded by the PPP2R5B gene.

USP6

Ubiquitin carboxyl-terminal hydrolase 6 (USB6), also termed TRE17 and Tre-2, is a deubiquitinating enzyme that in humans is encoded by the homanid USP6 gene located at band 13.2 on the short arm of chromosome 17. Deubiquitinating enzymes (DUBs) are enzymes that act within cells to remove ubiquitins from various functionally important proteins. Ubiquitin enzymes add ubiquitin to these proteins and thereby regulate their cellular location, alter their activity, and/or promote their degradation. By deubiquitinating these proteins, DUBs counter the effects of the ubiquinating enzymes and contribute to regulating the actions of the targeted proteins. In normal adult tissues, USP6 is highly expressed in testicle tissue, modestly expressed in ovarian tissue, and absent or minimally expressed in other tissues. It is also highly expressed in fetal brain tissue. The specific functions of USP6 are poorly defined primarily because its presence is restricted to primates: there are no available animal models to determine the effects of its deletion, although some studies suggest that UPSP6 contributes to normal brain development. In all events, USP6 has gained wide interest because of its abnormally increased expression by the neoplastic cells in various tumors derived from mesenchymal tissue.

PPP2R5E

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform is an enzyme that in humans is encoded by the PPP2R5E gene.

PPP4C

Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the PPP4C gene.

PPP2R3B Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta is an enzyme that in humans is encoded by the PPP2R3B gene.

PPP6C

Serine/threonine-protein phosphatase 6 catalytic subunit is an enzyme that in humans is encoded by the PPP6C gene.

PPP4R1

Serine/threonine-protein phosphatase 4 regulatory subunit 1 is an enzyme that in humans is encoded by the PPP4R1 gene.

PPP2R3C

Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma is an enzyme that in humans is encoded by the PPP2R3C gene.

Protein phosphatase 2

Protein phosphatase 2 (PP2), also known as PP2A, is an enzyme that in humans is encoded by the PPP2CA gene. The PP2A heterotrimeric protein phosphatase is ubiquitously expressed, accounting for a large fraction of phosphatase activity in eukaryotic cells. Its serine/threonine phosphatase activity has a broad substrate specificity and diverse cellular functions. Among the targets of PP2A are proteins of oncogenic signaling cascades, such as Raf, MEK, and AKT, where PP2A may act as a tumor suppressor.

Protein phosphatase 1

Protein phosphatase 1 (PP1) belongs to a certain class of phosphatases known as protein serine/threonine phosphatases. This type of phosphatase includes metal-dependent protein phosphatases (PPMs) and aspartate-based phosphatases. PP1 has been found to be important in the control of glycogen metabolism, muscle contraction, cell progression, neuronal activities, splicing of RNA, mitosis, cell division, apoptosis, protein synthesis, and regulation of membrane receptors and channels.

Proliferative fasciitis and proliferative myositis (PF/PM) are rare benign soft tissue lesions that increase in size over several weeks and often regress over the ensuing 1–3 months. The lesions in PF/PM are typically obvious tumors or swellings. Historically, many studies had grouped the two descriptive forms of PF/PM as similar disorders with the exception that proliferative fasciitis occurs in subcutaneous tissues while proliferative myositis occurs in muscle tissues. In 2020, the World Health Organization agreed with this view and defined these lesions as virtually identical disorders termed proliferative fasciitis/proliferative myositis or proliferative fasciitis and proliferative myositis. The Organization also classified them as one of the various forms of the fibroblastic and myofibroblastic tumors.

References

  1. ↑ "PPP6R3 – Gene – NCBI".
  2. ↑ "USP6 ubiquitin specific peptidase 6 [Homo sapiens (Human)] - Gene – NCBI".
  3. 1 2 Teramura Y, Yamazaki Y, Tanaka M, Sugiura Y, Takazawa Y, Takeuchi K, Nakayama T, Kaneko T, Musha Y, Funauchi Y, Ae K, Matsumoto S, Nakamura T (December 2019). "Case of mesenchymal tumor with the PPP6R3-USP6 fusion, possible nodular fasciitis with malignant transformation". Pathology International. 69 (12): 706–709. doi:10.1111/pin.12851. PMID   31538390. S2CID   202701385.
  4. ↑ "PPP6R3 – Serine/Threonine-protein phosphatase 6 regulatory subunit 3 – Homo sapiens (Human) – PPP6R3 gene & protein".
  5. ↑ Kitamura N, Fujiwara N, Hayakawa K, Ohama T, Sato K (July 2021). "Protein phosphatase 6 promotes neurite outgrowth by promoting mTORC2 activity in N2a cells". Journal of Biochemistry. 170 (1): 131–138. doi:10.1093/jb/mvab028. PMID   34314486.
  6. 1 2 Guo R, Wang X, Chou MM, Asmann Y, Wenger DE, Al-Ibraheemi A, Molavi DW, Aboulafia A, Jin L, Fritchie K, Oliveira JL, Jenkins RB, Westendorf JJ, Dong J, Oliveira AM (August 2016). "PPP6R3-USP6 amplification: Novel oncogenic mechanism in malignant nodular fasciitis". Genes, Chromosomes & Cancer. 55 (8): 640–9. doi:10.1002/gcc.22366. PMID   27113271. S2CID   4378693.
  7. ↑ Nakayama S, Nishio J, Aoki M, Koga K, Nabeshima K, Yamamoto T (2021). "Ubiquitin-specific Peptidase 6 (USP6)-associated Fibroblastic/Myofibroblastic Tumors: Evolving Concepts". Cancer Genomics & Proteomics. 18 (2): 93–101. doi:10.21873/cgp.20244. PMC   7943209 . PMID   33608306.
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