Literature: A-K ; L-Z ; subject area
Compiled by: Julian Thorpe
Pin1 Protein: General
Pin1 and Cancer ; Our Publications ; References
Pin1 is a protein of the parvulin family
within the peptidyl-prolyl cis-trans isomerase (PPIase)
group of proteins and was the first member of this family to
be found in humans (Lu et al. 1996 ; Crenshaw et al.
1998 ).
 | The PPIases are chaperone proteins
with a range of cellular functions which include modulating
the assembly, folding and transport of essential cellular proteins
at different subcellular locations which reflects the diversity
of their target proteins. |
| N.B. For more background on PPIases, please see one of my collaborator's site: |
Stuart Rulten's D. Phil thesis 'Characterisation of Novel Human PPIases'
|
The protein Pin1
is a recently characterised human PPIase ( Lu et al.,
1996 ) which modulates the assembly, folding, activity and
transport of essential cellular proteins. It is a mitotic regulator,
interacting with a range of proteins that are phosphorylated
prior to cell division ( Shen et al. 1998). Pin1 recognises
a specific motif of a phosphorylated serine or threonine
residue preceding a proline (Ser/Thr-Pro). Lu (2000)
suggests that phosphorylation-dependent prolyl isomerization
(by Pin1) may be a novel post-translational cell cycle regulatory
mechanism which organises the phosphorylated proteins into
a defined set of mitotic structural modifications. Lu also suggests
the potential of Pin1 as a drug target (because of its involvement
in mitotic arrest and apoptosis). |
| In common with other PPIases, Pin1 catalyses
the cis-trans isomerisation of proline-containing peptides and
recognises a specific motif of a phosphorylated serine or
threonine residue preceding a proline (Ser/Thr-Pro).
Since its characterisation, Pin1 has been the subject of intensive
research in a number of groups (e.g. Shen et al. 1998
). |
| Pin1 is a preferentially
nuclear protein which can regulate entry
of cells into mitosis and whose PPIase activity is required for
normal progression through mitosis in yeast and mammalian cells
( Lu et al. 1996; Lu and Hunter 1995; Fujimori et al., 1999
). Indeed, deletion of Pin1 activity in HeLa cells causes mitotic
arrest and apoptosis ( Lu et al. 1996 ). In addition to
binding to the targets of the mitotic phosphoprotein monoclonal-2 antibody
(MPM-2), Pin1 specifically interacts with and regulates the activity
of a subset of mitotic and nuclear proteins in a phosphorylation-dependent
manner ( Yaffe et al. 1997 ). In addition to having a
role in pre-mRNA 3’ end formation ( Morris et al. 1999), it
appears that nuclear localised Pin1 modulates the structure of target
proteins by isomerising phosphorylated serine/threonine bonds, and
is thereby intimately involved in regulating many aspects of cell cycle
control. (Also see Lu et al. 1999b; Patra et al. 1999 ). |
|
As stated above, in HeLa cells, Pin1 depletion causes
mitotic arrest and apoptosis
, whilst overexpression results in G2 phase arrest
( Lu et al., 1996). |
| Pin1 is itself regulated by PKA
(Lu
et al., 2002). Phosphorylation of its WW
domain (at Ser-16) by PKA abolishes the interactions between Pin1
and its target proteins. It was also demonstrated
that Pin1 is dephosphorylated in a cell cycle-regulated
manner, with the appearance of a faster-migrating band at mitosis. |
| Pin1 is additionally regulated by Plk1 (Eckerdt
et al. 2005). Phosphorylation at Ser-65 by Plk1 increases Pin1 stability by
inhibiting its ubiquitination. |
| Other work has revealed that Pin1 is overexpressed in breast cancer ( Wulf et al., 2001 ); it was suggested that this overexpression promotes oncogenesis through the interaction of Pin1 with c-Jun, thereby increasing the latter’s transcriptional activity, resulting in increased cellular levels of cyclin D1. N.B. on this latter point, Liou et al. (2002) have now reported that Pin1 binds to, and positively regulates the function of, cyclin D1 at both transcriptional and post-translational levels. They showed that binding of Pin1 stabilised cyclin D1 and suggested that this might be mediated via the prevention of its export from the nucleus (and subsequent proteolysis in the cytoplasm). |
Conversely, Pin1 has also been shown to have a potential anti-cancer role by regulating the apoptotic response to genotoxic insults via its interaction with the tumour suppressor protein p53 (Wulf et al., 2002 ; Zacchi et al., 2002 ; Zheng et al., 2002).
| Protein | Full name/Function | Reference(s) |
| APP | amyloid protein precursor (110kDa) | Davies et al., 2000 |
| Bcl-2 | apoptosis suppressor (26kDa) | Pathan et al., 2001 |
| Bcl-6 | transcription factor | Phan et al., 2007 |
| beta-catenin | oncogenic transcriptional activator (92kDa) | Ryo et al., 2001 |
| BimEL | BH3-only protein (pro-apoptotic) | Becker and Bonni, 2006 |
| Bruton tyrosine kinase (Btk) | Mutations in Btk cause X-linked agammaglobulinemia in humans | Yu et al., 2006 |
| Cdc25 | cell-cycle protein phosphatase (Cdc25C = 65kDa) | Crenshaw et al. 1998 ; Shen et al. 1998 |
| Cdc27 | component of anaphase-promoting complex [APC] (97kDa) | Shen et al. 1998 |
| Che-1 | a RNA polymerase II binding protein which plays an important role in transcriptional activation of p53 and in maintenance of the G2/M checkpoint | De Nicola et al. 2007 |
| c-Jun | mediates transcriptional regulation (35-39kDa) | Wulf et al., 2001 |
| CK2 | protein kinase (35/36kDa) | Messenger et al., 2002 |
| c-Myc | proto-oncogenic transcription factor | Dominguez-Sola and Dalla-Favera, 2004 |
| CRMP4 | collapsin response mediator protein 4 | Rembutsu et al., 2008 |
| Cyclin D1 |
cell cycle
regulator; aberrantly overexpressed in several human malignancies, e.g. breast cancer (34kDa) |
Liou et al., 2002 |
| Cyclin E(-Cdk2 complex) | cell cycle regulator | Yeh et al., 2006 |
| Daxx | death-associated protein | Ryo et al., 2007 |
| Emi1 | cell cycle regulator | Bernis et al., 2007 |
| Gephyrin | microtubule binding protein | Zita et al., 2007 |
| hSpt5 | subunit of the DRB sensitivity-inducing factor [DSIF] (175kDa) | Lavoie et al., 2001 |
| IRF3 | interferon-regulatory factor 3 (mediates interferon beta production) | Saitoh et al., 2006 |
| KRMP1 | kinesin-related protein (c.220kDa) | Kamimoto et al., 2001 |
| Mcl-1 | myeloid cell leukemia sequence-1 | Li et al., 2007 |
| Myt1 | cdc2 inhibitory kinase; inhibition of G2/M progression (c.55-60kDa) | Shen et al. 1998 ; Wells et al. 1999 |
| Nek6 | a human NIMA-related kinase | Chen et al., 2006 |
| Neurofilament Heavy Chain (NF-H) | neuronal cytoskeletal type IV intermediate filament | Kesavapany et at., 2007 |
| NFAT | nuclear factor of activated T cells (120kDa) | Liu et al., 2001 |
| NHERF-1 | Na+/H+ exchanger regulatory factor 1; a PDZ domain-containing adaptor protein known to bind to various receptors, channels, cytoskeletal elements, and cytoplasmic signaling proteins; a cdc2 kinase target showing 'association with Pin1' (c.52kDa) | He et al., 200 |
| the NIMA kinase | cell-cycle kinase; may have a role in G2/M progression | Lu et al. 1996 |
| Pim-1 | serine threonine protein kinase | Ma et al., 2007 |
| PKCa | protein kinase | Shen et al., 2008 |
| Plk1 | polo-like kinase 1 ; mitotic role (64kDa) | Crenshaw et al. 1998 ; Shen et al. 1998 |
| PML | Promyelocytic leukemia protein | Reineke et al., 2008 |
| p53 | tumour suppressor (53kDa) | Wulf et al., 2002 ; Zacchi et al., 2002 ; Zheng et al., 2002 |
| p54(nrb) |
transcription,
pre-mRNA processing, nuclear retention of edited |
Proteau et al. 2005 |
| p65/NF-kappaB | transcriptional factor | Ryo et al., 2003 |
| p66(Shc) | growth factor adapter (66kDa) | Pinton et al., 2007 |
| p70/p85S6K | kinase; phosphorylates the ribosomal protein S6 (70/85kDa) | Yaffe et al., 1997 |
| p73 | inducer of apoptosis | Mantovani et al. 2004 |
| Rab4 | GTP[guanosine triphosphate]-binding (21/22kDa) | Gerez et al. 2000 |
| Raf-1 kinase |
Raf-1
kinase: signaling molecule, |
Dougherty et al. 2005 |
| RARa | Retinoic Acid Receptor a: nuclear receptor that functions as a ligand-dependent transcription factor. | Brondani et al. 2005 |
| RNA polymerase II | transcription initiator (210-220kDa) | Albert et al. 1999 ; Morris et al. 1999 |
| Sil | SIL phosphorylation and interactions with PIN1 is required for maintenance of the mitotic checkpoint (148kDa) | Campaner et al. 2005 |
| Stat3 | Signal transducer and activator of transcription 3; cytoplasmic transcription factor important for cytokine signaling | Lufei et al., 2007 |
| Synphilin-1 | An alpha-synuclein (PARK1) and parkin (PARK2) interacting protein | Ryo et al. 2006 |
| Tau | microtubule-associated protein | Lu et al., 1999a ; Smet et al. 2004 |
| tis21 | implicated in the process of neurogenesis as a mediator of growth arrest before differentiation | Hong et al. 2005 |
| Topoisomerase IIa | changes the degree of DNA supercoiling, crucial for transcription and replication (c.200kDa) | Yaffe et al., 1997 |
| Wee1 | cell-cycle protein kinase (105kDa) | Shen et al. 1998 |
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Hashemzadeh-Bonehi L, Phillips RG, Cairns NJ, Mosaheb S, Thorpe JR (In Press) Pin1 protein associates with neuronal lipofuscin: potential consequences in age-related neurodegeneration. E
Thorpe
JR, Mosaheb S, Hashemzadeh-Bonehi L, Cairns NJ, Kay KE, Morley SJ, Rulten S (2004)
Shortfalls in the Peptidyl-Prolyl Cis-Trans
Isomerase Protein Pin1 in Neurons are Associated With Frontotemporal
Dementias. Neurobiology of Disease
THORPE, J.R.
,
MORLEY, S.J.
and
RULTEN, S.L.
(2001) (read
Abstract
)
Utilising the Peptidyl-Prolyl Cis-Trans Isomerase
Pin1 as a Probe of its Phosphorylated Target Proteins: Examples
of Binding to Nuclear Proteins in a Human Kidney Cell Line and
to Tau in Alzheimer’s Diseased Brain.
J. Histochem. Cytochem. 49: 97-108
THORPE,
J.R.
,
RULTEN, S.L.
and
KAY, J.E.
(1999) (read
Abstract
)
The binding of a putative and a known chaperone
protein revealed by immunogold labelling transmission electron
microscopy: A suggested use of chaperones as probes for the distribution
of their target proteins.
J. Histochem. Cytochem. 47, 1633-1640
RULTEN,
S.L.
,
THORPE, J.R.
and
KAY, J.E.
(1999) (read
Abstract
)
Identification of Eukaryotic Parvulin Homologues:
A new subfamily of peptidyl-prolyl cis-trans isomerases.
Biochem Biophys Res Comm 259: 557-562
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Akiyama H, Shin R-W, Uchida C, Kitamtoto T, Uchida T (2005) Pin1 promotes production of Alzheimer's amyloid b from b-cleaved amyloid precursor protein. Biochemical and Biophysical Research Communications 336: 521-529
Albert A, Lavoie S, Vincent M (1999) A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1. J Cell Science 112: 2493-2500
Albert, AL, Lavoie, SB, Vincent, M (2004) Multisite phosphorylation of Pin1-associated mitotic phosphoproteins revealed by monoclonal antibodies MPM-2 and CC-3. BMC CELL BIOLOGY 5: 10-22
An, WL, Cowburn, RF,
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(2003)
Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to
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163: 591-607
Anderson, AJ, Su, JH and Cotman, CW (1996) DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. JOURNAL OF NEUROSCIENCE 16: 1710-1719
Arevalo-Rodriguez, M, Cardenas, ME, Wu, XY, Hanes, SD and Heitman, J (2000) Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO JOURNAL 19: 3739-3749
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Atchison, FW, Means, AR (2003) Spermatogonial depletion in adult Pin1-deficient mice. BIOLOGY OF REPRODUCTION 69: 1989-1997
Atchison, FW, Means, AR (2004) A role for Pin1 in mammalian germ cell development and spermatogenesis. FRONTIERS IN BIOSCIENCE 9: 3248-3256
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(2003)
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