
Tgif1 is essential for osteoblasts to adapt a regular cell morphology, efficiently adhere and migrate on collagen type I-rich matrices, and activate bone surfaces during bone regeneration and in response to parathyroid hormone treatment.


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Osteoblast adherence to bone surfaces is important for remodeling of the bone tissue. This study demonstrates that deficiency of TG-interacting factor 1 (Tgif1) in osteoblasts results in altered cell morphology, reduced adherence to collagen type I-coated surfaces, and impaired migration capacity. Tgif1 is essential for osteoblasts to adapt a regular cell morphology and to efficiently adhere and migrate on collagen type I-rich matrices in vitro . Furthermore, Tgif1 acts as transcriptional repressor of p21-activated kinase 3 (PAK3), an important regulator of focal adhesion formation and osteoblast spreading. Absence of Tgif1 leads to increased PAK3 expression, which impairs osteoblast spreading. Additionally, Tgif1 is implicated in osteoblast recruitment and activation of bone surfaces in the context of bone regeneration and in response to parathyroid hormone 1-34 (PTH 1-34) treatment in vivo . These findings provide important novel insights in the regulation of the cytoskeletal architecture of osteoblasts.

### Competing Interest Statement

The authors have declared no competing interest.

Tgif1-deficiency impairs cytoskeletal architecture in osteoblasts by activating PAK3 signaling

tgif1-deficiency-impairs-osteoblast-cytoskeletal-architecture-and-bone-regeneration


Tgif1 Deficiency Impairs Osteoblast Cytoskeletal Architecture and Bone Regeneration
