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1 Supplementary Figure 1. Functional enrichment analyses of secretomic proteins. (a) Significant biological processes (upper panel) and disease biomarkers (lower panel) 2

2 involved by hrab37-mediated secretory proteins. P values are shown as -log. Gene number shown in green represents the number of genes from secretomic dataset that are involved in the indicated pathways or diseases. Gene number shown in red represents total number of genes that are involved in the indicated pathways or diseases by Metacore software-based analysis. (b) An enrichment map was constructed using Cytoscape installed with the Enrichment Map plugin. Node represents each enriched GO term obtained by Fisher s exact test with FDR (P < 0.05) and overlap cutoff > Node size is proportional to the total number of genes in each GO term. Edge thickness represents the number of overlapping genes between nodes. GO terms of similar functions are sorted into one cluster, marked with circles and labels. 3

3 Supplementary Figure 2. hrab37-mediated secretion of TIMP1 and TNF- is blocked by EXO1 treatment. (a) Immunoblots of TIMP1 secretion level in CM of cells treated with exocytosis inhibitor EXO1. (b) TNF- secretion level in CM of cells treated with EXO1 was analyzed by TNF- ELISA kit. 4

4 Supplementary Figure 3. Functional hrab37 localizes to the cytosol with vesicle binding affinity. (a) Immuno-EM images show a decreased amount of hrab37 (18 nm of gold) in the cytosolic region and vesicle binding in T43N compared to WT and Q89L cells. Names of organelles and location of the hrab37 gold particles are defined below the images. For example, red and black arrows indicate cytosol hrab37 with or without vesicle binding, respectively. Scale bars: 500 nm. (b,c) Quantitation of localization of hrab37 (b) and vesicle docking affinity (c) in cell images are shown as a percentage in the graph. Each measurement is the average of 1000 hrab37 gold particles. Data are mean ± s.e.m. (n = 2). P values determined using two-tailed Student s t-test. 5

5 Supplementary Figure 4. Rab8a does not regulate TIMP1 trafficking in CL1-5 cells. (a) Confocal microscopy images of RAB8a (red), hrab37 (red), TIMP1 (green) and nucleus staining (blue) in RAB8a and WT-hRAB37 expressed CL1-5 cells. Enlarged images shown in the insets of the merged panel. Scale bars: 10 μm. Rab8a (#1 and #2) did not co-localize with TIMP1 as seen in the WT-hRAB37 expressed cells. (b) Vesicles in CL1-5 cells, expressing Flag-tagged RAB8a or Flag-tagged hrab37 protein, were immunoprecipitated (IP) with anti-flag beads and the lysates were blotted for endogenous TIMP1 and Flag-tagged RAB8a or hrab37. TIMP1 was associated with hrab37-containing vesicles but not with Rab8a-containing vesicles. (c) Immuno-EM images show localization of RAB8a or hrab37 (10 nm of gold, arrow) and TIMP1 (15 nm of gold, arrow head) in RAB8a and WT-hRAB37 expressed cells. Scale bars: 100 nm. Rab8a and TIMP1 were distributed to distinct regions in cells. (d) Immunoblots showed that higher concentrations of TIMP1 in conditioned medium (CM) from hrab37 cells compared to control and Rab8a cells. 6

6 Supplementary Figure 5. Immunofluorescence microscopy images of ectopically expressed vector-gfp and -RFP in CL1-5 cells. To demonstrate the fluorescence signals spatially, CL1-5 cells co-transfected with (a) vector-gfp and (b) vector-rfp imaged by fluorescence microscopy taken together with our TIRF analysis are shown. (c) is the merge image. Scale bars: 10 μm. 7

7 Supplementary Figure 6. hrab37 mediates TIMP1 secretion to inhibit motility in A549 and H460 lung cancer cells. (a,c) Transwell invasion assays H460 (a) and A549 (c) cells expressing WT hrab37. Scale bars: 100 μm. Invasion abilities in H460 and A549 were quantified and normalized to control group shown as a percentage in the graph (bottom). P values determined using two-tailed Student s t-test. Data represent mean ± s.e.m. (n = 3). (b,d) Immunoblots of H460 (b) and A549 (d) for cytosolic expression of hrab37 and -actin as well as TIMP1 secretion in CM are shown. Gelatin-zymography assay for MMP9 activity are shown with pro-form and active form of MMP9 labeled as indicated. 8

8 Supplementary Figure 7. hrab37 inhibits the activity of p-fak and RhoA in vitro and in vivo. (a) Representative immunoblots of p-fak and total FAK of lysates from control, WT, Q89L and T43N CL1-5 cells are shown (upper panel). RhoA activity assay of lysates from control, WT, Q89L and T43N CL1-5 cells is shown (lower panel). (b) Immunohistochemistry was performed in lung tissues from control, WT, Q89L and T43N mice to detect the expression levels of p-fak protein. The insets (right, scale bars: 450 μm) are a higher magnification of the boxed areas (left, scale bars: 150 μm). (c) Representative immunoblots of p-fak and total FAK of lysates from knockdown control (sh-con.) and stable hrab37 knockdown clones 1 and 2 (sh1 and sh2) H460 cells are shown (upper panel). RhoA activity assay of lysates from sh-con, sh1 and sh2 H460 cells (lower panel). 9

9 Supplementary Figure 8. Knockdown of ectopically expressed WT hrab37 increased cell migration and invasion ability in CL1-5 cells. (a,b) Migration (a) and invasion (b) assay in WT and WT-hRAB37KD CL1-5 cells. Scale bars: 100 μm. The migration and invasion abilities were quantified and normalized to control group shown as a percentage in the graph (right). P values determined using two-tailed Student s t-test. Data represent mean ± s.e.m. (n = 3). (c) Immunoblots for cytosolic expression of hrab37 and -actin as well as TIMP1 secretion in CM are shown. Gelatin-zymography assay for MMP9 activity are also shown with pro-form and active form of MMP9 labeled as indicated. 10

10 Supplementary Figure 9. hrab37 inhibits lung cancer motility in vitro via TIMP1 (a) Immunoblots for cytosolic expression of TIMP1 and β-actin are shown. (b,c) Migration (b) and invasion (c) assays of Q89L-hRAB37 (Q89L-Con), TIMP1KD (Q89L-TIMP1KD) and reconstituted TIMP1 by adding TIMP1 recombinant protein (Q89L-TIMP1KD+TIMP1). Scale bars: 100 μm. Q89L-TIMP1KD showed an increase in cell migration and invasion, whereas Q89L-TIMP1KD+TIMP1 abolished the migration and invasion ability. The migration and invasion abilities were quantified and normalized to control group and shown as a percentage in the graph (right). P values determined using two-tailed Student s t-test. Data represent mean ± s.e.m. (n = 3). 11

11 Supplementary Figure 10. TIMP1 treatment abolishes lung cancer metastasis of T43N cells in vitro and in vivo. (a,b) Transwell migration (a) and invasion (b) assays in hrab37 T43N CL1-5 cells (T43N) and T43N cells treated with TIMP1 recombinant protein (+TIMP1). Scale bars: 100 μm. The migration and invasion abilities were quantified and normalized to control group shown as a percentage in the graph (right). P values were calculated by two-tailed Student s t test. Data represent mean ± s.e.m. (n = 3). (c) Four representative lung images from mice intravenously 12

12 injected via tail-vein with CL1-5 cells expressing hrab37 T43N or treating with TIMP1. A total of six mice per group were analyzed. (d) H&E stains of lung tissues taken from mice tail-vein injected with cells indicated. Scale bars: 400 μm. Tumor nodule numbers of T43N and +TIMP1 mice groups are shown in the graph (right). Data are mean ± s.e.m. P values were calculated by two-tailed Student s t-test (n = 6 mice per group). 13

13 Supplementary Figure 11. hrab37 correlates with TIMP1 expression in lung cancer patients. (a) Fluorescence immunohistochemistry of hrab37 (red), TIMP1 (green) and nucleus staining (blue) in five specimens from normal lung tissue from tissue arrays. (b) Fluorescence immunohistochemistry of hrab37 (red), TIMP1 (green) and nucleus staining (blue) in lung cancer patients from tissue arrays. Upper: ten 14

14 patients expressed both hrab37 and TIMP1 proteins. Lower: another ten showed low expression of hrab37 and concordantly reduced TIMP1 expression in their tumor tissue. Scale bar: 20 μm. 15

15 Supplementary Figure 12. hrab37 does not affect cell growth ability in vitro and in vivo. (a) Proliferation ability of control and WT-hRAB37 expressed CL1-5 cells as measured by MTT assay. Cell viability were detected at 24, 48 and 72 h. P values determined using two-tailed Student s t-test. Data are mean ± s.e.m. (n = 3). (b) Three representative tumor tissue images from mice injected subcutaneously with CL1-5 cells expressing control and WT-hRAB37. A total of five mice per group were analyzed. Scale bars: 1 cm. (c) Tumor weights in the control and WT mice groups are shown in the graph. Data are mean ± s.e.m. P values were calculated by two-tailed Student s t-test (n = 5 mice per group). 16

16 Supplementary Figure 13. Colon and liver cancer tissues express low level of hrab37 mrna. (a,b) Semi-quantitative RT-PCR assay from representative paired primary normal (N) and tumor (T) tissues from colon (a) and liver (b) cancer patients. The tumor tissues expressing low amounts of hrab37 mrna are indicated with arrows. GAPDH was used as internal control. 17

17 Supplementary Figure 14. TIMP1 is not present in hrab37-containing vesicles of RCC cells. (a,b) Immunoblots of TIMP1 secretion level in CM from renal cell carcinoma cells Caki-1 (a) and 786-O (b) expressing control vector or hrab37 vector are shown. TIMP1 level in CM was not changed in these cells expressing either control or hrab37 vector. (c,d) Vesicles of Caki-1 (c) and 786-O (d) cells, expressing Flag-tagged hrab37 protein, were immunoprecipitated (IP) with anti-flag beads and lysates were blotted for Flag-tagged hrab37 and endogenous TIMP1. TIMP1 was not associated with hrab37-containing vesicles in these cells. 18

18 Supplementary Figure 15. The hrab37 antibody developed shows high specificity. Cell lysates from CL1-5 control (lane 1), CL1-5 hrab37-wt (lane 2), and hrab37kd in the WT-hRAB37 background (WT-hRAB37KD, lane 3) cells were subjected to immunoblotting analysis using hrab37 antibody (LTK BioLaboratories) to detect the total hrab37 or Flag-tag antibody to detect the ectopic hrab37. -actin was used as loading control. The results showed that hrab37 antibody specifically recognized WT-hRAB37 (lane 2), while the signal was reduced in WT-hRAB37KD (lane 3). Immunoblotting using Flag-tag antibody showed similar results. Arrow indicates the predicted molecular weight of hrab37. 19

19 Supplementary Figure 16. Full-length images of representative immunoblots. 20

20 Supplementary Figure 16. Continued 21

21 Supplementary Table 1. Clinicopathological parameters in lung cancer patients enrolled in this study. Total patient number (N= 165) Characteristics* N % Age < > Sex Male Female Smoke Yes No Unknown Tumor type ADC SCC Others Tumor stage I II III IV T status T T T T N status N N M status M M * ADC: adenocarcinoma, SCC: squamous cell carcinoma, T describes the size of the tumor, N describes regional lymph nodes, M describes distant metastasis. 22

22 Supplementary Table 2. Antibodies and their reaction conditions used in the present study. Target K.D. Raised In Application* Dilution Source Catalog No. -actin 42 Mouse WB 1:5000 Abcam ab3280 DAPI IF 1:5000 Sigma Aldrich D8417 EEA1 180 Mouse IF 1:100 BD Biosciences Flag -- Rabbit WB 1:1000 Santa Cruz sc-807 Flag -- Mouse IP 1:1000 Sigma F1804 hrab37 30 Mouse WB, IF, IHC, EM 1:500; 1:200; 1:400; 1:50 LTK BioLaboratories Homemade IGG 150 Mouse IP 1:1000 Millipore p-fak 125 Rabbit WB, IHC 1:1000; 1:100 Abcam ab4803 FAK 125 Mouse WB 1:1000 Abcam ab28152 RhoA 21 Mouse WB 1:500 Cytoskeleton #ARH03 TIMP1 34 Rabbit WB, IF, IP, EM TIMP1 34 Rabbit IHC 1:100 1:500; 1:200; 1:500; 1:50 Epitomic 2109-S Spring Bioscience E3364 Fluor Rabbit IF, IHC 1:1000 Invitrogen A11008 Fluor Rabbit IF 1:1000 Invitrogen A11035 Fluor Mouse IF, IHC 1:1000 Invitrogen A nm immune- Gold 15nm immune- Gold 10nm immune- Gold -- Mouse Immuno-EM 1:10 Abcam ab Rabbit Immuno-EM 1:10 BBInternational EM GAR15 -- Mouse Immuno-EM 1:10 Abcam Ab27241 * WB: western blot, IF: immunofluorescence, IP: immunoprecipitation, IHC: immunohistochemistry, EM: electron microscope. -- Molecular weight is variable. -- It is used for nuclear staining. The specificity of in-house generated hrab37 antibody is shown in Supplementary Figure

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