These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin.
    Author: Mues A, van der Ven PF, Young P, Fürst DO, Gautel M.
    Journal: FEBS Lett; 1998 May 22; 428(1-2):111-4. PubMed ID: 9645487.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]