CLP-36 PDZ-LIM Protein Associates with Nonmuscle α-Actinin-1 and α-Actinin-4

Vallenius, Tea; Luukko, Keijo; Mäkelä, Tomi P.

doi:10.1074/jbc.275.15.11100

Cited by 138 publications

(161 citation statements)

References 34 publications

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“…59 PDLIM1 could function as a cytoskeletal organization scaffold and an adaptor for the recruitment of several factors. For example, PDLIM1 interacted with F-actin-based stress fibers via an association with nonmuscle ACTN1 and ACTN4 in nonmuscle tissues, 48 and PDLIM1 formed a triple complex with ACTN1 and PALLD in stress fibers. 60 In adult rat testes, PALLD colocalizes with EPS8 which is an actin filamentbundling and barbed end-capping protein and ACTR3, which is abranched actin polymerization protein, suggesting that it might regulate actin filament bundle dynamics at the ectoplasmic specialization in the epithelial cycle of spermatogenesis.…”

Section: Discussionmentioning

confidence: 99%

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Autophagy is required for ectoplasmic specialization assembly in sertoli cells

et al. 2016

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The ectoplasmic specialization (ES) is essential for Sertoli-germ cell communication to support all phases of germ cell development and maturity. Its formation and remodeling requires rapid reorganization of the cytoskeleton. However, the molecular mechanism underlying the regulation of ES assembly is still largely unknown. Here, we show that Sertoli cell-specific disruption of autophagy influenced male mouse fertility due to the resulting disorganized seminiferous tubules and spermatozoa with malformed heads. In autophagy-deficient mouse testes, cytoskeleton structures were disordered and ES assembly was disrupted. The disorganization of the cytoskeleton structures might be caused by the accumulation of a negative cytoskeleton organization regulator, PDLIM1, and these defects could be partially rescued by Pdlim1 knockdown in autophagy-deficient Sertoli cells. Altogether, our works reveal that the degradation of PDLIM1 by autophagy in Sertoli cells is important for the proper assembly of the ES, and these findings define a novel role for autophagy in Sertoli cell-germ cell communication.

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Section: Discussionmentioning

confidence: 99%

“…6A and 6C). As PDLIM1 is a member of the PDZ and LIM protein family that could associate with F-actin by interacting with ACTN1and ACTN4, 48 we focused on PDLIM1 as a candidate negative regulator that participated in the process of autophagy-modulated cytoskeleton organization. …”

Section: Overexpression Of Pdlim1 Affects the Structure Organization mentioning

confidence: 99%

Autophagy is required for ectoplasmic specialization assembly in sertoli cells

et al. 2016

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“…PDLIM1, 2, 3, 4, and 6 all bind a-actinin via their PDZ domain and are involved with recruitment of LIM-binding proteins to the cytoskeleton. [13][14][15][16][17][18] PDLIM7 is known to bind b-tropomyosin via its PDZ domain and, therefore, also acts to direct LIM-binding proteins to the cytoskeleton. 19 A similar association has not yet been observed for PDLIM5, which is, however, of interest due to its potential as a susceptibility gene for schizophrenia.…”

Section: Introductionmentioning

confidence: 99%

Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms

et al. 2010

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PDZ domains most commonly bind the C-terminus of their protein targets. Typically the C-terminal four residues of the protein target are considered as the binding motif, particularly the C-terminal residue (P0) and third-last residue (P-2) that form the major contacts with the PDZ domain's ''binding groove''. We solved crystal structures of seven human PDZ domains, including five of the seven PDLIM family members. The structures of GRASP, PDLIM2, PDLIM5, and PDLIM7 show a binding mode with only the C-terminal P0 residue bound in the binding groove. Importantly, in some cases, the P-2 residue formed interactions outside of the binding groove, providing insight into the influence of residues remote from the binding groove on selectivity. In the GRASP structure, we observed both canonical and noncanonical binding in the two molecules present in the asymmetric unit making a direct comparison of these binding modes possible. In addition, structures of the PDZ domains from PDLIM1 and PDLIM4 also presented here allow comparison with canonical binding for the PDLIM PDZ domain family. Although influenced by crystal packing arrangements, the structures nevertheless show that changes in the positions of PDZ domain side-chains and the aB helix allow noncanonical binding interactions.

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“…Several PDZ-LIM proteins have been detected in the muscle Z-line and shown to interact with ␣-actinin (5)(6)(7)(8)(9)(10)(11)(12). PDZ domain is a widely expressed protein-protein interaction domain (for review, see Ref.…”

mentioning

confidence: 99%

“…Actinin-associated LIM protein (ALP) 1 (5,10), C-terminal LIM domain protein (CLP36) (14) (also called hCLIM1 (15) or Elfin (16)), Reversion-induced LIM protein (RIL) (17), and Mystique (Uniprot accession number Q7Z584) belong to the first class, which has one N-terminal PDZ domain and one C-terminal LIM domain. ALP is expressed in muscle (5,10), whereas CLP36 and RIL are mainly expressed in nonmuscle tissues (11,18,19). CLP36 shows also high expression levels in muscle (7,15,16).…”

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confidence: 99%

The ZASP-like Motif in Actinin-associated LIM Protein Is Required for Interaction with the α-Actinin Rod and for Targeting to the Muscle Z-line

Klaavuniemi

Kelloniemi

Ylänne

2004

Journal of Biological Chemistry

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The Z-line is a specialized structure connecting adjacent sarcomeres in muscle cells. ␣-Actinin cross-links actin filaments in the Z-line. Several PDZ-LIM domain proteins localize to the Z-line and interact with ␣-actinin. Actinin-associated LIM protein (ALP), C-terminal LIM domain protein (CLP36), and Z band alternatively spliced PDZ-containing protein (ZASP) have a conserved region named the ZASP-like motif (ZM) between PDZ and LIM domains. To study the interactions and function of ALP we used purified recombinant proteins in surface plasmon resonance measurements. We show that ALP and ␣-actinin 2 have two interaction sites. The ZM motif was required for the interaction of ALP internal region with the ␣-actinin rod and for targeting of ALP to the Z-line. The PDZ domain of ALP bound to the C terminus of ␣-actinin. This is the first indication that the ZM motif would have a direct role in a proteinprotein interaction. These results suggest that the two interaction sites of ALP would stabilize certain conformations of ␣-actinin 2 that would strengthen the Z-line integrity.The muscle Z-line is a highly specialized structure between adjacent sarcomeres in muscle fibers that maintain the organization of the contractile machinery (for review, see Ref. 1). ␣-Actinin is one of the major components at the Z-line. The ␣-actinin polypeptide is composed of an N-terminal actin binding domain, four spectrin repeats that form the central rod region (2, 3), and two pairs of C-terminal EF-hands (4). ␣-Actinin forms an antiparallel homodimer. ␣-Actinin cross-links actin filaments from opposite sarcomeres to the Z-line and, therefore, has a major mechanical function in keeping the sarcomeres together.Several PDZ-LIM proteins have been detected in the muscle Z-line and shown to interact with ␣-actinin (5-12). PDZ domain is a widely expressed protein-protein interaction domain (for review, see Ref. 13). PDZ-LIM proteins form one subgroup of PDZ proteins (13) and are regarded as mediators between cytoskeletal structures and signaling cascades.PDZ-LIM proteins can be divided in two subclasses; they either contain one or three LIM domains. Actinin-associated LIM protein (ALP) 1 (5, 10), C-terminal LIM domain protein (CLP36) (14) (also called hCLIM1 (15) or Elfin (16)), Reversion-induced LIM protein (RIL) (17), and Mystique (Uniprot accession number Q7Z584) belong to the first class, which has one N-terminal PDZ domain and one C-terminal LIM domain. ALP is expressed in muscle (5, 10), whereas CLP36 and RIL are mainly expressed in nonmuscle tissues (11,18,19). CLP36 shows also high expression levels in muscle (7,15,16). Enigma, Enigma homology protein, and ZASP/Cypher/Oracle form the second class, with one N-terminal PDZ domain and three C-terminal LIM domains. They all are expressed mainly in muscle (6, 9, 20 -22). An interesting feature of these seven PDZ-LIM proteins is that ALP, CLP36, and ZASP contain a conserved region, named ZASP-like motif (ZM) (SMART prediction (23) accession number SM 00735, Interpro 006643), in the internal r...

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CLP-36 PDZ-LIM Protein Associates with Nonmuscle α-Actinin-1 and α-Actinin-4

Cited by 138 publications

References 34 publications

Autophagy is required for ectoplasmic specialization assembly in sertoli cells

Autophagy is required for ectoplasmic specialization assembly in sertoli cells

Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms

The ZASP-like Motif in Actinin-associated LIM Protein Is Required for Interaction with the α-Actinin Rod and for Targeting to the Muscle Z-line

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