SUMO1

Case Study 1: Andreia Lee, 2019

Conjugation of small ubiquitin-like modifiers (SUMOs) to substrate proteins is a posttranslational protein modification that affects a diverse range of physiological processes. Global inhibition of SUMO conjugation in mice results in embryonic lethality, reflecting the importance of the SUMO pathways for embryonic development. Here, the researchers demonstrated that SUMO1 overexpression was not well tolerated in murine embryonic carcinoma and embryonic stem (ES) cells and that only a few clones were recovered after transduction with vectors delivering SUMO1 expression constructs. Differentiated NIH/3T3 cells overexpress SUMO1 without deleterious effects and maintain high levels of both conjugated and free forms of SUMO1. The few embryonic cells surviving after forced overexpression retained all their SUMO1 in the form of a few high-molecular-weight conjugates and maintained undetectable levels of free SUMO1. The absence of free SUMO in embryonic cells was seen specifically upon overexpression of SUMO1, but not SUMO2. Moreover, blocking SUMO1 conjugation to endogenous substrates by C-terminal mutations of SUMO1 or by overexpression of a SUMO1 substrate "sponge" or by overexpression of the deSUMOylating enzyme SUMO-specific peptidase 1 (SENP1) dramatically restored free SUMO1 overexpression.

Fig1. Western blot of lysates of embryonic cell lines (F9, PCC4, and E14 cells) transduced with vectors expressing either Flag-SUMO1 or Flag-SUMO1ΔGG.

Fig2. Western blot analysis of F9 cells engineered by successive transductions to coexpress Flag-SUMO1 (WT) or Flag-SUMO1ΔGG (ΔGG) along with HA-Trim28 (WT) or HA-Trim286KR (6KR).

Case Study 2: Changkang Ke, 2019

One previous study showed that SUMO1 expression is closely related to progression in non-small cell lung cancer (NSCLC); however, the function of SUMO1 in NSCLC has not yet been well elucidated. SUMO1 was enhanced or silenced in two NSCLC cell lines by using either forced SUMO1 expression or short hairpin RNA against SUMO1 lentiviral vectors, respectively. The biological functions of SUMO1 in NSCLC were investigated through colony-formation, cell proliferation, and invasion assays, and cell cycle analysis. NF-κB expression was detected in the overexpressed and silenced SUMO1 cell lines. Immunohistochemistry was used to detect an association between SUMO1 and NF-κB in the cancer and adjacent tissues of 168 patients with lung cancer. The results showed overexpressed SUMO1 promoted the proliferation rate, colony formation ability, invasion, and NF-κB expression in an A549 cell line. Conversely, SUMO1 depletion inhibited the cell growth rate, colony formation ability, invasion, and NF-κB expression in a Calu-1 cell line.

Fig3. Similar results were obtained through Western blot analysis.

Fig4. Forced expression of SUMO1 increased the number of A549 cells in the S phase of the cell cycle.

Fig1. Schematic diagram of the effect and molecular mechanism of Smad2 SUMOylation in the progression of TGF-β-induced EndoMT. (Qi Su, 2023)

Fig2. Model of the effects of SUMO1 on the Wnt/β-Catenin signaling pathway in relation to colitis. (Jingyan Wang, 2020)

SUMO1 involved in several pathways and played different roles in them. We selected most pathways SUMO1 participated on our site, such as RNA transport, which may be useful for your reference. Also, other proteins which involved in the same pathway with SUMO1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

SUMO1 has several biochemical functions, for example, SUMO transferase activity, ion channel binding, poly(A) RNA binding. Some of the functions are cooperated with other proteins, some of the functions could acted by SUMO1 itself. We selected most functions SUMO1 had, and list some proteins which have the same functions with SUMO1. You can find most of the proteins on our site.

SUMO1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with SUMO1 here. Most of them are supplied by our site. Hope this information will be useful for your research of SUMO1.

UBE2I; DAXX; SP100