Table 1 Studies related to p53 aggregation

TAD (AA1–70)

Segment (AA1–63)

Under acidic conditions, it can aggregate into amyloid assemblies in vitro, and the aggregates are toxic to human SH-SY5Y cells

[51]

DBD (AA 94–293)

p53C (AA94–312)

Tendency to aggregate in vitro, same state of p53C and R248Q under pressure and high temperature; Exogenous addition of synthesized p53 core fibrils (seeds) in vitro can induce aggregation of the endogenous wild-type p53 in normal cells; In cellulo model of full-length p53 amyloid formation, the mechanism of loss of p53 tumorsuppressive function with concomitant oncogenic gain of functions, the mechanism of the transformation of cells due to p53 amyloids leading to cancer pathogenesis was established

[6, 23, 46]

Segment (AA251–257)

The aggregation-nucleating segment is predicted to be a key region of p53 aggregation and has been confirmed by in vitro and in vivo experiments, and mutation I254R can inhibit aggregation

[8, 22, 52, 53]

R175H

Weak oligomerization tendency in vivo; ApoDBD can initiate aggregation of zinc-bound DBD through the nucleation growth process

[18, 54]

R248Q

Moderate oligomerization tendency in vivo; R248Q mutant aggregates exhibit GOF and DN effects

[13, 18]

R273H

Strong tendency to aggregate in the body

[18]

H193L, I195L, Y234C, G245S, wild-type

Small amounts of aggregates are present in the body, and tumor aggressiveness is strongly correlated with p53 aggregation

[18]

OD (AA324–355)

Full-length,N-terminal truncation (AA93–393)

After induction of aggregation in vitro, aggregates can penetrate cells through macrocytic drinking action and co-aggregation with cellular p53

[55]

G334V

In vitro G334V peptide forms amyloid aggregates and hetero-oligomers with wild-type peptides through a two-step process

[56]

R337H

In vitro R337H has a higher propensity to form amyloidogenic fibrils than wild-type p53

[57]