Group:MUZIC:ZASP: Difference between revisions

Line 24:

==Function and Interactions==

PDZ domains are known to target proteins to sites of complex formation, as such ZASP functions most probably as the '''oracle''' of Z-disk multi-protein complexes by tethering and regulating interacting proteins via its PDZ and LIM domains. This is suggested by experimental evidences which show the PDZ domain of ZASP interacts with myotilin, FATZ protein family and α-actinin-2. Based on interaction with the class I PDZ-binding motif (PBM) of α-actinin-2, the PDZ domain of ZASP is categorised as a typical class I interaction module. A recent report on the interaction of ZASP PDZ domain with class III PBMs in myotilin and myozenin suggests that ZASP PDZ domain has dual capacity (or classification) and possible structural plasticity as it is able to bind both class I and class III motifs<ref name="b" /> from three different proteins. Apart from the PDZ domain, ZASP's internal motif (the ZASP-like motif) confers the ability to interact with the spectrin repeats of α-actinin-2 <ref>doi:10.1016/j.yexcr.2005.12.036</ref>. In addition, there is increasing evidence that ZASP also performs signaling functions; the LIM domains of cypher (the mouse orthologue of ZASP) binds and directs PKC to the Z-disk, with mutation affecting this interaction <ref>PMID:10391924</ref>.

PDZ domains are known to target proteins to sites of complex formation, as such ZASP functions most probably as the '''oracle''' of Z-disk multi-protein complexes by tethering and regulating interacting proteins via its PDZ and LIM domains. This is suggested by experimental evidences which show the PDZ domain of ZASP interacts with myotilin, FATZ protein family and α-actinin-2. Based on interaction with the class I PDZ-binding motif (PBM) of α-actinin-2, the PDZ domain of ZASP is categorised as a typical class I interaction module. A recent report on the interaction of ZASP PDZ domain with class III PBMs in myotilin and myozenin suggests that ZASP PDZ domain has dual capacity (or classification) and possible structural plasticity as it is able to bind both class I and class III motifs<ref name="b" /> from three different proteins. Apart from the PDZ domain, ZASP's internal motif (the ZASP-like motif) confers the ability to interact with the spectrin repeats of α-actinin-2 <ref name= "xp">doi:10.1016/j.yexcr.2005.12.036</ref>. In addition, there is increasing evidence that ZASP also performs signaling functions; the LIM domains of cypher (the mouse orthologue of ZASP) binds and directs PKC to the Z-disk, with mutation affecting this interaction <ref>PMID:10391924</ref>.

==Pathology==

Group:MUZIC:ZASP: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 24: / Line 24: @@
 ==Function and Interactions==
-PDZ domains are known to target proteins to sites of complex formation, as such ZASP functions most probably as the '''oracle''' of Z-disk multi-protein complexes by tethering and regulating interacting proteins via its PDZ and LIM domains. This is suggested by experimental evidences which show the PDZ domain of ZASP interacts with myotilin, FATZ protein family and α-actinin-2. Based on interaction with the class I PDZ-binding motif (PBM) of α-actinin-2, the PDZ domain of ZASP is categorised as a typical class I interaction module. A recent report on the interaction of ZASP PDZ domain with class III PBMs in myotilin and myozenin suggests that ZASP PDZ domain has dual capacity (or classification) and possible structural plasticity as it is able to bind both class I and class III motifs<ref name="b" /> from three different proteins. Apart from the PDZ domain, ZASP's internal motif (the ZASP-like motif) confers the ability to interact with the spectrin repeats of α-actinin-2 <ref>doi:10.1016/j.yexcr.2005.12.036</ref>.  In addition, there is increasing evidence that ZASP also performs signaling functions; the LIM domains of cypher (the mouse orthologue of ZASP) binds and directs PKC to the Z-disk, with mutation affecting this interaction <ref>PMID:10391924</ref>.
+PDZ domains are known to target proteins to sites of complex formation, as such ZASP functions most probably as the '''oracle''' of Z-disk multi-protein complexes by tethering and regulating interacting proteins via its PDZ and LIM domains. This is suggested by experimental evidences which show the PDZ domain of ZASP interacts with myotilin, FATZ protein family and α-actinin-2. Based on interaction with the class I PDZ-binding motif (PBM) of α-actinin-2, the PDZ domain of ZASP is categorised as a typical class I interaction module. A recent report on the interaction of ZASP PDZ domain with class III PBMs in myotilin and myozenin suggests that ZASP PDZ domain has dual capacity (or classification) and possible structural plasticity as it is able to bind both class I and class III motifs<ref name="b" /> from three different proteins. Apart from the PDZ domain, ZASP's internal motif (the ZASP-like motif) confers the ability to interact with the spectrin repeats of α-actinin-2 <ref name= "xp">doi:10.1016/j.yexcr.2005.12.036</ref>.  In addition, there is increasing evidence that ZASP also performs signaling functions; the LIM domains of cypher (the mouse orthologue of ZASP) binds and directs PKC to the Z-disk, with mutation affecting this interaction <ref>PMID:10391924</ref>.
 ==Pathology==