Phosphatase Subfamily TAB1 - Revision history

Gerard: /* Human TAB1 is a pseudophosphatase but basal metazoan TAB1s are probably active */

2017-03-04T00:25:30Z

‎Human TAB1 is a pseudophosphatase but basal metazoan TAB1s are probably active

Gerard: /* Domain */

2017-03-04T00:24:34Z

‎Domain

Gerard at 18:31, 6 March 2016

2016-03-06T18:31:15Z

Mark: /* References */

2015-10-02T17:50:10Z

‎References

Mark: /* Domain */

2015-10-02T17:49:56Z

‎Domain

Gerard: /* Evolution */

2015-06-18T17:47:51Z

‎Evolution

Gerard: /* Evolution */

2015-06-18T17:47:19Z

‎Evolution

Gerard: /* Evolution */

2015-06-18T17:46:52Z

‎Evolution

Gerard: /* TAB1 binds to TAK1 and induces its autophosphorylation */

2015-06-18T17:44:08Z

‎TAB1 binds to TAK1 and induces its autophosphorylation

Gerard at 17:39, 18 June 2015

2015-06-18T17:39:21Z

@@ Line 13: / Line 13: @@
 ===== Human TAB1 is a pseudophosphatase but basal metazoan 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 <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. D69 is found in invertebrates, including 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  =====

@@ Line 8: / Line 8: @@
 === Domain ===
-The TAB1 subfamily has a phosphatase domain of PPM fold and a conserved C-terminal motif to bind TAK1, which has a pattern of PYVDXA/TXF <cite> Ono01</cite>. The phosphatase domain binds to X-linked inhibitor of apoptosis (XIAP) <cite>Lu07</cite>.
+TAB1 has a PPM-fold phosphatase domain and a C-terminal TAK1-binding motif motif (PYVDxA/TxF) <cite> Ono01</cite>. The phosphatase domain binds to X-linked inhibitor of apoptosis (XIAP) <cite>Lu07</cite>.
 === Function ===

@@ Line 12: / Line 12: @@
 === Function ===
-===== Human TAB1 is a pseudophosphatase but basal metazoa TAB1s are probably active =====
+===== Human TAB1 is a pseudophosphatase but basal metazoan 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 <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 binds to TAK1 and induces its autophosphorylation  =====
-Human TAB1 physically associates with TAK1 <cite>Shibuya96</cite> and induces TAK1 autoactivation <cite>Sakurai00, Scholz10</cite>. Similar results have been also observed with he respective C. elegans orthologs, tap-1 and mom-4 <cite>Meneghini99, Smit04</cite>.
+TAB1 physically associates with TAK1 <cite>Shibuya96</cite> and induces TAK1 autoactivation, both in human <cite>Sakurai00, Scholz10</cite> and C. elegans <cite>Meneghini99, Smit04</cite>.
-TAB1 has a conserved C-terminal region of about 30 AA, including a PYVDXA/TXF, motif, found to mediate TAK1 interaction in vertebrates and nematodes <cite>Sakurai00, Ono01</cite>. In addition, the association with TAK1 is isoform specific. TAB1β is a splice isoform of TAB1,in which the C-terminal 69 amino acids of TAB1α were replaced with an unrelated 27-amino acid sequence. This does not interact with TAK1 <cite>Ge03</cite>. Taken together, the interaction between TAB1α and TAK1 is mediated by the C-terminal motif.
+TAB1 has a conserved C-terminal region of about 30 AA, including a PYVDXA/TXF, motif, found to mediate TAK1 interaction in vertebrates and nematodes <cite>Sakurai00, Ono01</cite>. This association is isoform specific: the TAB1β splice isoform replaces the the C-terminal 69 AA with an unrelated 27 AA sequence. This does not interact with TAK1 <cite>Ge03</cite>.
 ===== 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>.
+Human TAB1 associates with p38α in complex with TRAF6 <cite>Ge02</cite> and induces its autophosphorylation <cite>Tanno03</cite>. p38α binds to both the isoforms TAB1α and TAB1β <cite>Ge03</cite>.
 * 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.

@@ Line 36: / Line 36: @@
 #Ge03 pmid=12429732
 #Lanna14 pmid=25151490
 #Meneghini99 pmid=10391246
 #Ono01 pmid=11323434

@@ Line 8: / Line 8: @@
 === Domain ===
-The TAB1 subfamily has a phosphatase domain of PPM fold and a conserved C-terminal motif to bind TAK1, which has a pattern of PYVDXA/TXF <cite> Ono01</cite>.
+The TAB1 subfamily has a phosphatase domain of PPM fold and a conserved C-terminal motif to bind TAK1, which has a pattern of PYVDXA/TXF <cite> Ono01</cite>. The phosphatase domain binds to X-linked inhibitor of apoptosis (XIAP) <cite>Lu07</cite>.
 === Function ===

@@ Line 3: / Line 3: @@
 === 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 kinases from the MAPK cascade, [http://www.kinase.com/wiki/index.php/Kinase_Subfamily_TAK1 TAK1] and [http://www.kinase.com/wiki/index.php/Kinase_Subfamily_p38 p38] 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 TAB1 modulation of TAK1 and p38.
+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 kinases from the MAPK cascade, [http://www.kinase.com/wiki/index.php/Kinase_Subfamily_TAK1 TAK1] and [http://www.kinase.com/wiki/index.php/Kinase_Subfamily_p38 p38] 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 TAB1 modulation of TAK1 and p38.
 Human TAB1 can be phosphorylated at Ser-452, Ser-453, Ser-456, Ser-457 by TAK1 and p38 <cite>Wolf11</cite>. This stretch of serines is not found in invertebrates.

@@ Line 5: / Line 5: @@
 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 kinases from the MAPK cascade, [http://www.kinase.com/wiki/index.php/Kinase_Subfamily_TAK1 TAK1] and [http://www.kinase.com/wiki/index.php/Kinase_Subfamily_p38 p38] 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 TAB1 modulation of TAK1 and p38.
-Human TAB1 can be dephosphorylated at Ser-452, Ser-453, Ser-456, Ser-457 by TAK1 and p38 <cite>Wolf11</cite>. This stretch of series is not found in invertebrates.
+Human TAB1 can be phosphorylated at Ser-452, Ser-453, Ser-456, Ser-457 by TAK1 and p38 <cite>Wolf11</cite>. This stretch of series is not found in invertebrates.
 === Domain ===