Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with α-actinin—Analysis of patient mutations

Klaavuniemi, Tuula; Ylänne, Jari

doi:10.1016/j.yexcr.2005.12.036

Cited by 53 publications

(47 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…14 ZASP contains a PDZ motif at its N-terminus, which interacts with C-terminus of α-actinin-2, 12 and a conserved sequence called the ZASPlike motif (ZM) found in the alternatively spliced exons 4 and 6. 15 It has also been reported to bind to the FATZ (calsarcin) family of Z-disc proteins 16 …”

Section: The Sarcomerementioning

confidence: 99%

Cytoskeletal Basis of Ion Channel Function in Cardiac Muscle

Vatta

Faulkner

2006

Future Cardiol.

View full text Add to dashboard Cite

SummaryThe heart is a force-generating organ that responds to self-generated electrical stimuli from specialized cardiomyocytes. This function is modulated by sympathetic and parasympathetic activity.In order to contract and accommodate the repetitive morphological changes induced by the cardiac cycle, cardiomyocytes depend on their highly evolved and specialized cytoskeletal apparatus. Defects in components of the cytoskeleton, in the long term, affect the ability of the cell to compensate at both functional and structural levels. In addition to the structural remodeling, the myocardium becomes increasingly susceptible to altered electrical activity leading to arrhythmogenesis. The development of arrhythmias secondary to structural remodeling defects has been noted, although the detailed molecular mechanisms are still elusive. Here I will review the current knowledge of the molecular and functional relationships between the cytoskeleton and ion channels and, I will discuss the future impact of new data on molecular cardiology research and clinical practice.

show abstract

Section: The Sarcomerementioning

confidence: 99%

Cytoskeletal Basis of Ion Channel Function in Cardiac Muscle

Vatta

Faulkner

2006

Future Cardiol.

View full text Add to dashboard Cite

show abstract

“…More than 15 mutations in ZASP have been reported resulting in a range of myopathies including DCM [11,175], HCM [176], MFM [177], inclusion body myositis [178], and LVNCC [11,175,177] (Table 5). ZASP contains a PDZ domain, located at the N-terminus, and an internal ZASP/cypher-like motif (ZM) both capable of interacting with -Actinin-2 [179][180][181]. Additionally, the PDZ domain interacts with Myotilin [158] and FATZ [182], which provides structural stability to the Z-disk.…”

Section: Zasp and Zaspopathiesmentioning

confidence: 99%

Myofibrillar Myopathies and the Z-Disk Associated Proteins

Ruparelia¹,

Vaz²,

Bryson-Richardson³

2012

Skeletal Muscle - From Myogenesis to Clinical Relations

View full text Add to dashboard Cite

“…The largest isoforms have three C-terminal LIM (LIN-11, Isl1m, MEC-3 proteins) domains that interact with Protein kinases C (PKCs) (Zhou et al, 1999). ZASP proteins were shown to localize at the Z disc (Klaavuniemi & Ylanne, 2006). The first case of ZASPopathy causing MFM was described in 2005 in 11 MFM patients carrying heterozygous missense mutations (Selcen & Engel, 2005).…”

Section: Zaspmentioning

confidence: 99%