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Two immunoglobulin‐like domains of the Z‐disc portion of titin interact in a conformation‐dependent way with telethonin
Author(s) -
Mues Alexander,
van der Ven Peter F.M,
Young Paul,
Fürst Dieter O,
Gautel Mathias
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00501-8
Subject(s) - titin , obscurin , immunoglobulin domain , phosphorylation , chemistry , microbiology and biotechnology , sarcomere , biochemistry , biophysics , biology , myocyte , gene
The giant muscle protein titin/connectin plays a crucial role in myofibrillogenesis as a molecular ruler for sarcomeric protein sorting. We describe here that the N‐terminal titin immunoglobulin domains Z1 and Z2 interact specifically with telethonin in yeast two‐hybrid analysis and protein binding assays. Immunofluorescence with antibodies against the N‐terminal region of titin and telethonin detects both proteins at the Z‐disc of human myotubes. Longer titin fragments, comprising a serine‐proline‐rich phosphorylation site and the next domain, do not interact. The interaction of telethonin with titin is therefore conformation‐dependent, reflecting a possible phosphorylation regulation during myofibrillogenesis.