Difference between revisions of "Phosphatase Subfamily TAB1"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPM|Fold PPM (PP2C)]]: [[Phosphatase_Superfamily_PPM|Superfamily PPM (PP2C)]]: [[Phosphatase_Family_PPM|Family PPM (PP2C)]]: [[Phosphatase_Subfamily_TAB1|Subfamily TAB1]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPM|Fold PPM (PP2C)]]: [[Phosphatase_Superfamily_PPM|Superfamily PPM (PP2C)]]: [[Phosphatase_Family_PPM|Family PPM (PP2C)]]: [[Phosphatase_Subfamily_TAB1|Subfamily TAB1]] | ||
=== Evolution === | === Evolution === | ||
| + | The TAB1 subfamily is found throughout metazoa. It was lost in Drosophila, but is present in most other arthropods (see [http://resdev.gene.com/gOrtholog/view/cluster/MC0007029/overview internal data]. Its interacting partners, two MAPKs, TAK1/MAP3K7 and p38α/MAPK14 emerged earlier, in [[Phosphatase_Glossary#Holozoa|holozoa]] and [[Phosphatase_Glossary#Opisthokont|opisthokont]], respectively. Interestingly, they are present in Drosophila, which suggests Drosophila may lose the modulation of TAB1 over TAK1 and p38. | ||
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| + | Human TAB1 can be dephosphorylated at Ser-452, Ser-453, Ser-456, Ser-457 by TAK1 and p38 <cite>Wolf11</cite>. But, the stretch of serines are not found in invertebrates. | ||
=== Domain === | === Domain === | ||
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Human TAB1 is a pseudophosphatase. Several key residues required for dual metal-binding (D69N, D290E, D356E, N367D) and catalysis (H71Y) are substitued by other amino acids <cite>Conner06</cite>. However, not all of the substitutions are conserved in TAB1s. D69 is found in metazoa, such as sponge, nematostella and sea urchin; D290 is found in metazoa except chordates, such as sponge, nematostella and C. elegans; D356 is found in metazoa, such as sponge, nematostella and sea urchin; H71 is found in basal metazoa, such as nematostella and sponge. Thus, TAB1s in basal metazoa are probably active, though human TAB1 is inactive. | Human TAB1 is a pseudophosphatase. Several key residues required for dual metal-binding (D69N, D290E, D356E, N367D) and catalysis (H71Y) are substitued by other amino acids <cite>Conner06</cite>. However, not all of the substitutions are conserved in TAB1s. D69 is found in metazoa, such as sponge, nematostella and sea urchin; D290 is found in metazoa except chordates, such as sponge, nematostella and C. elegans; D356 is found in metazoa, such as sponge, nematostella and sea urchin; H71 is found in basal metazoa, such as nematostella and sponge. Thus, TAB1s in basal metazoa are probably active, though human TAB1 is inactive. | ||
| − | ===== TAB1 | + | ===== TAB1 binds to TAK1 and induces its autophosphorylation ===== |
| − | Human TAB1 | + | Human TAB1 associates with TAK1 <cite>Shibuya96</cite> and induces TAK1 autoactivation <cite>Sakurai00, Scholz10</cite>. Similar results have been also observed in C. elegans, between tap-1 and mom-4, which are the orthologs of TAB1 and TAK1, respectively <cite>Meneghini99, Smit04</cite>. |
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| + | TAB1 has a conserved C-terminal motif (last 30 amini acids), PYVDXA/TXF, among mammalian TAB1, Xenopus TAB1 and, C.elegans tap-1 <cite>Sakurai00, Ono01</cite>. In addition, the association with TAK1 is isoform specific. TAB1α but not TAB1β interacts with TAK1. The two isoforms are identical except the C-terminal 69 amino acids of TAB1α were replaced with an unrelated 27-amino acid sequence <cite>Ge03</cite>. Taken together, the interaction between TAB1α and TAK1 is mediated by the C-terminal motif. | ||
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| + | ===== TAB1 binds to p38α and induces its autophosphorylation ===== | ||
| + | Human TAB1 associates with p38α in complex with TRAF6 <cite>Ge02</cite> and induces its autophosphorylation <cite>Tanno03</cite>. In contrast with TAK1, which only binds to TAB1α, p38α binds to both the isoforms TAB1α and TAB1β <cite>Ge03</cite>. | ||
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* p38α <cite>Ge02, Zhu13, Lanna14</cite>. TAB1 functions as a scaffold protein in the activation of p38 <cite>Lanna14</cite>. The interaction between TAB1 and p38α is mediated by Pro-412 on TAB1 and a hydrophobic docking groove on p38α <cite>Zhou06</cite>. The Pro-412 of TAB1 does not localize in a conserved region, so it is hard to tell whether it is conserved. | * p38α <cite>Ge02, Zhu13, Lanna14</cite>. TAB1 functions as a scaffold protein in the activation of p38 <cite>Lanna14</cite>. The interaction between TAB1 and p38α is mediated by Pro-412 on TAB1 and a hydrophobic docking groove on p38α <cite>Zhou06</cite>. The Pro-412 of TAB1 does not localize in a conserved region, so it is hard to tell whether it is conserved. | ||
| + | ===== Other interacting partners: XIAP and MEKK1 ===== | ||
* MEKK1 <cite>Charlaftis14</cite>. TAB1 is ubiquitinated by MEKK1 PHD domain. | * MEKK1 <cite>Charlaftis14</cite>. TAB1 is ubiquitinated by MEKK1 PHD domain. | ||
| + | * X-chromosome-linked inhibitor of apoptosis protein (XIAP) <cite>Yamaguchi99</cite>. | ||
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=== References === | === References === | ||
<biblio> | <biblio> | ||
#Charlaftis14 pmid=25260751 | #Charlaftis14 pmid=25260751 | ||
#Conner06 pmid=16879102 | #Conner06 pmid=16879102 | ||
| − | #Ge02 pmid=12429732 | + | #Ge02 pmid=11847341 |
| + | #Ge03 pmid=12429732 | ||
#Lanna14 pmid=25151490 | #Lanna14 pmid=25151490 | ||
| + | #Meneghini99 pmid=10391246 | ||
| + | #Ono01 pmid=11323434 | ||
| + | #Sakurai00 pmid=10838074 | ||
#Scholz10 pmid=20538596 | #Scholz10 pmid=20538596 | ||
#Shibuya96 pmid=8638164 | #Shibuya96 pmid=8638164 | ||
| + | #Smit04 pmid=14960582 | ||
| + | #Tanno03 pmid=12829618 | ||
| + | #Yamaguchi99 pmid=9878061 | ||
#Zhou06 pmid=16648477 | #Zhou06 pmid=16648477 | ||
#Zhu14 pmid=23934659 | #Zhu14 pmid=23934659 | ||
</biblio> | </biblio> | ||
Revision as of 17:56, 9 June 2015
Phosphatase Classification: Fold PPM (PP2C): Superfamily PPM (PP2C): Family PPM (PP2C): Subfamily TAB1
Contents
Evolution
The TAB1 subfamily is found throughout metazoa. It was lost in Drosophila, but is present in most other arthropods (see internal data. Its interacting partners, two MAPKs, TAK1/MAP3K7 and p38α/MAPK14 emerged earlier, in holozoa and opisthokont, respectively. Interestingly, they are present in Drosophila, which suggests Drosophila may lose the modulation of TAB1 over TAK1 and p38.
Human TAB1 can be dephosphorylated at Ser-452, Ser-453, Ser-456, Ser-457 by TAK1 and p38 [1]. But, the stretch of serines are not found in invertebrates.
Domain
The TAB1 subfamily has a phosphatase domain of PPM fold.
Function
Human TAB1 is a pseudophosphatase but basal metazoa TAB1s are probably active
Human TAB1 is a pseudophosphatase. Several key residues required for dual metal-binding (D69N, D290E, D356E, N367D) and catalysis (H71Y) are substitued by other amino acids [2]. However, not all of the substitutions are conserved in TAB1s. D69 is found in metazoa, such as sponge, nematostella and sea urchin; D290 is found in metazoa except chordates, such as sponge, nematostella and C. elegans; D356 is found in metazoa, such as sponge, nematostella and sea urchin; H71 is found in basal metazoa, such as nematostella and sponge. Thus, TAB1s in basal metazoa are probably active, though human TAB1 is inactive.
TAB1 binds to TAK1 and induces its autophosphorylation
Human TAB1 associates with TAK1 [3] and induces TAK1 autoactivation [4, 5]. Similar results have been also observed in C. elegans, between tap-1 and mom-4, which are the orthologs of TAB1 and TAK1, respectively [6, 7].
TAB1 has a conserved C-terminal motif (last 30 amini acids), PYVDXA/TXF, among mammalian TAB1, Xenopus TAB1 and, C.elegans tap-1 [4, 8]. In addition, the association with TAK1 is isoform specific. TAB1α but not TAB1β interacts with TAK1. The two isoforms are identical except the C-terminal 69 amino acids of TAB1α were replaced with an unrelated 27-amino acid sequence [9]. Taken together, the interaction between TAB1α and TAK1 is mediated by the C-terminal motif.
TAB1 binds to p38α and induces its autophosphorylation
Human TAB1 associates with p38α in complex with TRAF6 [10] and induces its autophosphorylation [11]. In contrast with TAK1, which only binds to TAB1α, p38α binds to both the isoforms TAB1α and TAB1β [9].
- p38α [10, 12, 13]. TAB1 functions as a scaffold protein in the activation of p38 [13]. The interaction between TAB1 and p38α is mediated by Pro-412 on TAB1 and a hydrophobic docking groove on p38α [14]. The Pro-412 of TAB1 does not localize in a conserved region, so it is hard to tell whether it is conserved.
Other interacting partners: XIAP and MEKK1
- MEKK1 [15]. TAB1 is ubiquitinated by MEKK1 PHD domain.
- X-chromosome-linked inhibitor of apoptosis protein (XIAP) [16].
References
Error fetching PMID 16879102:
Error fetching PMID 11847341:
Error fetching PMID 12429732:
Error fetching PMID 25151490:
Error fetching PMID 10391246:
Error fetching PMID 11323434:
Error fetching PMID 10838074:
Error fetching PMID 20538596:
Error fetching PMID 8638164:
Error fetching PMID 14960582:
Error fetching PMID 12829618:
Error fetching PMID 9878061:
Error fetching PMID 16648477:
Error fetching PMID 23934659:
- Error fetching PMID 16879102:
- Error fetching PMID 8638164:
- Error fetching PMID 10838074:
- Error fetching PMID 20538596:
- Error fetching PMID 10391246:
- Error fetching PMID 14960582:
- Error fetching PMID 11323434:
- Error fetching PMID 12429732:
- Error fetching PMID 11847341:
- Error fetching PMID 12829618:
- Error fetching PMID 25151490:
- Error fetching PMID 16648477:
- Error fetching PMID 25260751:
- Error fetching PMID 9878061:
- Error fetching PMID 23934659:
