TY - JOUR AU - Kellermayer, Miklós AU - Granzier, HL TI - Calcium-dependent inhibition of in vitro thin-filament motility by native titin JF - FEBS LETTERS J2 - FEBS LETT VL - 380 PY - 1996 IS - 3 SP - 281 EP - 286 PG - 6 SN - 0014-5793 DO - 10.1016/0014-5793(96)00055-5 UR - https://m2.mtmt.hu/api/publication/1337556 ID - 1337556 AB - Titin (also known as connectin) is a giant filamentous protein that spans the distance between the Z- and NI-lines of the vertebrate muscle sarcomere and plays a fundamental role in the generation of passive tension. Titin has been shown to bind strongly to myosin, making it tightly associated to the thick filament in the sarcomere. Recent observations have suggested the possibility that titin also interacts with actin, implying further functions of titin in muscle contraction, We show - using in vitro motility and binding assays - that native titin interacts with both filamentous actin and reconstituted thin filaments. The interaction results in the inhibition of the filaments' in vitro motility. Furthermore, the thin-thin filament interaction occurs in a calcium-dependent manner: increased calcium results in enhanced binding of thin filaments to titin and greater suppression of in vitro motility. LA - English DB - MTMT ER - TY - JOUR AU - Stienen, G J M AU - Versteeg, P G A AU - Papp, Zoltán AU - Elzinga, G TI - MECHANICAL-PROPERTIES OF SKINNED RABBIT PSOAS AND SOLEUS MUSCLE-FIBERS DURING LENGTHENING - EFFECTS OF PHOSPHATE AND CA2+ JF - JOURNAL OF PHYSIOLOGY-LONDON J2 - J PHYSIOL-LONDON VL - 451 PY - 1992 SP - 503 EP - 523 PG - 21 SN - 0022-3751 UR - https://m2.mtmt.hu/api/publication/1005483 ID - 1005483 LA - English DB - MTMT ER -