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KIF22 – Spondyloepimetaphyseal Dysplasia with Multiple Dislocations

KIF22, encoding a kinesin‐like motor protein, is implicated in autosomal dominant spondyloepimetaphyseal dysplasia with multiple dislocations (MONDO:0011335). Affected individuals present postnatal short stature, midface hypoplasia, generalized joint laxity and progressive epimetaphyseal dysplasia. Radiographically, hallmark features include small and delayed epiphyses, metaphyseal striations and slender metacarpals. Genetic and experimental data converge to support a strong gene‐disease relationship, guiding diagnosis, management and genetic counselling.

1 Assess Clinical Validity

Genetic evidence encompasses 32 unrelated probands with heterozygous KIF22 missense variants (20 familial cases from eight families segregating disease) and robust functional concordance. The number of sporadic and familial cases (32 probands) (PMID:22152678) and segregation in eight families (PMID:22152678) support a Strong classification.

2 Genetic Evidence

Inheritance is autosomal dominant. Segregation analysis in eight multiplex families demonstrated co-segregation of KIF22 variants with disease in 20 additional affected relatives (PMID:22152678). Case reports include a de novo c.443C>T (p.Pro148Leu) variant in a child followed longitudinally from age 2 to 11 (PMID:25256152) and the same hotspot mutation in a 66-year-old man (PMID:37226647). Variant spectrum is dominated by adjacent missense changes at codons 148 and 149; recurrent alleles include c.443C>T (p.Pro148Leu), c.446G>A (p.Arg149Gln) and c.446G>T (p.Arg149Leu).

3 Functional / Experimental Evidence

Homozygous variants (c.146G>A, p.Arg49Gln) identified in three unrelated families cause a recessive form with similar clinical features, implicating haploinsufficiency and altered ATP binding (PMID:38477767). Patient fibroblasts show decreased sulfated proteoglycan secretion and reduced chondroitin sulfate deposition, linking KIF22 dysfunction to proteoglycan biosynthesis defects (PMID:38477767). In vitro knockdown and expression of SEMDJL2 mutants in chondrocytes disrupt spindle formation and proliferation; KIF22 truncation mice recapitulate growth plate abnormalities and shortened bones (PMID:38989461).

4 Conflicting Evidence

No studies to date have refuted the association or described alternative phenotypes for KIF22 variants in SEMDJL2.

5 Integration & Conclusion

Combined genetic and functional data demonstrate that heterozygous missense variants in KIF22, particularly at codons 148–149, cause autosomal dominant spondyloepimetaphyseal dysplasia with multiple dislocations via dominant‐negative or haploinsufficient mechanisms affecting chondrocyte division and proteoglycan biosynthesis. Recessive variants expand the allelic spectrum and underscore critical roles in skeletal development. This evidence supports genetic testing for KIF22 in patients with compatible skeletal dysplasia and informs prognosis and family counseling.

Key Take-home: Pathogenic KIF22 missense variants (e.g., c.443C>T (p.Pro148Leu)) cause autosomal dominant SEMDJL2 with characteristic skeletal abnormalities and impaired proteoglycan synthesis, warranting inclusion in diagnostic gene panels.

References

  • Pediatric radiology • 2015 • Spondyloepimetaphyseal dysplasia with joint laxity, leptodactylic type: longitudinal observation of radiographic findings in a child heterozygous for a KIF22 mutation. PMID:25256152
  • American journal of medical genetics. Part C • 2023 • Spondyloepimetaphyseal dysplasia with joint laxity type 2: Aggregating the literature and reporting on the life of a 66-year-old man. PMID:37226647
  • American journal of human genetics • 2011 • Recurrent dominant mutations affecting two adjacent residues in the motor domain of the monomeric kinesin KIF22 result in skeletal dysplasia and joint laxity. PMID:22152678
  • Journal of bone and mineral research • 2024 • Identification of kinesin family member (KIF22) homozygous variants in spondyloepimetaphyseal dysplasia with joint laxity, lepdodactylic type and demonstration of proteoglycan biosynthesis impairment. PMID:38477767
  • iScience • 2024 • KIF22 regulates mitosis and proliferation of chondrocyte cells. PMID:38989461

Evidence Based Scoring (AI generated)

Gene–Disease Association

Strong

32 probands ([PMID:22152678]), segregation in eight families ([PMID:22152678]), concordant functional data

Genetic Evidence

Strong

32 unrelated cases and familial segregation in eight families

Functional Evidence

Moderate

Proteoglycan biosynthesis impairment in patient cells and chondrocyte mitotic defects in models