Rho GTPase: Difference between revisions

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== Function ==

'''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''', '''RhoC''', '''RhoD''' and '''RhoE'''. These 3 proteins share 85% sequence identity. RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one. A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>. '''Mitochondrial Rho GTPase''' ('''Miro''') have tandem GTP-binding domains separated by a linker region containing calcium-binding EF hand motifs indicating a role in mitochondrial homeostasis and apoptosis<ref>PMID:12482879</ref>.

'''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''', '''RhoC''', '''RhoD''' and '''RhoE'''. These proteins share 85% sequence identity. RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one. A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>. '''Mitochondrial Rho GTPase''' ('''Miro''') have tandem GTP-binding domains separated by a linker region containing calcium-binding EF hand motifs indicating a role in mitochondrial homeostasis and apoptosis<ref>PMID:12482879</ref>.

== Disease ==

Rho GTPase: Difference between revisions

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 == Function ==
-'''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''', '''RhoC''', '''RhoD''' and '''RhoE'''.  These 3 proteins share 85% sequence identity.  RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers.  Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one.  A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>.  '''Mitochondrial Rho GTPase''' ('''Miro''') have tandem GTP-binding domains separated by a linker region containing calcium-binding EF hand motifs indicating a role in mitochondrial homeostasis and apoptosis<ref>PMID:12482879</ref>.
+'''Rho GTPase''' of higher vertebrates include '''RhoA, RhoB''', '''RhoC''', '''RhoD''' and '''RhoE'''.  These proteins share 85% sequence identity.  RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers.  Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one.  A number of proteins have been identified as targets of RhoA<ref>PMID:12642488</ref>.  '''Mitochondrial Rho GTPase''' ('''Miro''') have tandem GTP-binding domains separated by a linker region containing calcium-binding EF hand motifs indicating a role in mitochondrial homeostasis and apoptosis<ref>PMID:12482879</ref>.
 == Disease ==