Matsuda M , Chu CW , Sokol SY .

R35GM122492 NIH HHS , R35 GM122492 NIGMS NIH HHS , R01 NS100759 NINDS NIH HHS

             actomyosin contractile ring
             adherens junction
             ectoderm development
             myosin II heavy chain binding

	Figure 1. Lmo7 localizes at junctional actomyosin bundles in Xenopus ectoderm cells. (A-Q″) Xenopus embryos were injected into animal blastomeres with GFP-Lmo7 or Flag-Lmo7 RNA (200 pg) or GFP-NMIIA RNA (300 pg) as indicated and the superficial ectoderm was imaged at stage 11. Protein localization was evaluated by direct GFP fluorescence, or by indirect immunofluorescence for Flag-Lmo7, endogenous NMIIA, ZO-1 and β-catenin. (A) Peri-junctional GFP-Lmo7 localization. Areas marked by rectangles are enlarged in B and B′. (B) Peri-junctional double bands of GFP-Lmo7 are more evident in shorter cell-cell junctions. (B′) GFP-Lmo7 is enriched near tricellular junctions but excluded from them. (C,C′) Cryosections of the superficial layer of ectoderm showing GFP-Lmo7 localization at the most apical region of the lateral membrane (arrowheads), co-stained with phalloidin. (D-G″) Relative distribution of GFP-Lmo7 and endogenous ZO-1 in x-y view (D-E″) and x-z view (F-G″). Areas marked by rectangles in D-D″ and F-F″ are enlarged in E-E″ and G-G″, respectively. (H,H′) Relative localization of GFP-Lmo7 and endogenous β-catenin in x-z view. (I-J″) Relative localization of Flag-Lmo7 and GFP-NMIIA. Bi-cellular junctions and tricellular junctions marked by rectangles and squares in I-I″ are enlarged in J-J″ and K-K″, respectively. (L,M) Endogenous NMIIA localization. An area marked by a rectangle is enlarged in M. (N-O″) Relative localization of GFP-Lmo7 and endogenous NMIIA in x-z view. Areas marked by rectangles in N-N″ are enlarged in O-O″. (P-Q″) Relative localization of GFP-Lmo7 and F-actin. An area marked by a rectangle in P is enlarged in Q-Q″. (R) Quantification of GFP-Lmo7, NMIIA and F-actin fluorescence intensity near apical junctions. The cell-cell boundary is defined as 0 on the x-axis. GFP-Lmo7 is located closer to the cell-cell boundary (0.138 µm) than NMIIA (0.272 µm) (upper panel, n=28, P<0.001). There is no statistically significant difference between GFP-Lmo7 (0.139 µm) and F-actin (0.101 µm) (lower panel, n=16, P>0.25). Spearman's correlation coefficient is 0.9959 and 0.9879 in GFP-Lmo7 and NMIIA in the upper panel, and 0.9943 and 0.9968 in GFP-Lmo7 and F-actin in the lower panel. (S) Schematics of the relative distribution of Lmo7 in apical junctions. Scale bars: 10 µm in A,C,D,F,H,I,L,N,P; 2 µm in B,E,G,J,K,M,O,Q. Images shown are representative of two to five experiments.
	Figure 2. Lmo7 induces apical constriction in Xenopus ectoderm. (A,B) GFP-Lmo7 RNA (1 ng) was injected into two animal blastomeres of four- to eight-cell stage embryos. (A) Control uninjected embryo at stage 11. (B) Embryo expressing GFP-Lmo7 at stage 11 exhibiting apical pigment granule accumulation. (C,C′) Reduced apical domain in cells expressing GFP-Lmo7 (200 pg RNA) in stage 11 embryos. En face view of the ectoderm co-stained with phalloidin. Asterisks indicate GFP-Lmo7-expressing cells. (D) Quantification of apical domain surface size in cells expressing GFP-Lmo7 (n=101) and adjacent control cells (n=101). Images were taken from at least five embryos. (E-F′) Cross-sections of the ectoderm in stage 11 embryos expressing GFP-Lmo7 RNA (200 pg). Embryos were co-stained with phalloidin. Arrowheads indicate GFP-Lmo7 or F-actin accumulation at the most apical region of the basolateral membrane. (G) The ratio of the apical to the basolateral domain length in the cells expressing GFP-Lmo7 (n=49) and uninjected control cells (n=49). (H,H′) Increased apical domain in Lmo7-ATGMO cells. Lmo7-ATGMO (30 ng) was co-injected with membrane-tethered RNA (100 pg). The ectoderm from stage 11 embryos was co-stained with phalloidin, en face view. Asterisks indicate Lmo7-ATGMO-containing cells. (I) Quantification of apical domain size in Lmo7-ATGMO cells (n=58) and adjacent control cells (n=54). Images were taken from at least five embryos. Statistical significance of the difference between the median values was assessed by the Mann–Whitney U-test. Scale bars: 500 µm in A; 10 µm in C,E,F,H. Images shown are representative of two or three experiments.
	Figure 3. Lmo7 promotes actomyosin bundle formation at apical junctions. Effects of Flag-Lmo7 overexpression on peri-junctional actomyosin networks. Flag-Lmo7 RNA (1 ng) was injected into one blastomere of four- to eight-cell stage embryos. Stage 11 embryos were co-stained with phalloidin, anti-Flag, anti-pMRLC or anti-NMIIA antibodies, as indicated. The superficial ectoderm was imaged. (A-C″) F-actin bundle formation in cells expressing Flag-Lmo7. Areas marked by rectangles in A,A′ are enlarged in B-C″. (C-C″) Lmo7 double bands between two adjacent Flag-Lmo7-expressing cells overlap with F-actin double bands. There are periodic sarcomere-like structures (arrowheads). (D) Phalloidin fluorescence intensity was measured at the borders between two adjacent control cells (control) or two Lmo7-expressing cells (Lmo7OE). (E-G″) MRLC phosphorylation at Ser 20. Areas marked by rectangles in E-E′ are enlarged in F-G″. (H) Fluorescence intensity of pMRLC(S20) staining related to images in E-G″. (I-K″) NMIIA accumulation. Areas marked by rectangles are enlarged in J-K″. (L) Fluorescence intensity of NMIIA staining related to images in I-K″. The boxes and whiskers indicate the lower and upper quartiles, and variability outside the upper and lower quartiles. Statistical significance of the difference was assessed by the Mann–Whitney U-test. Scale bars: 10 µm in A,E,I; 2 µm in B,C,F,G,J,K. Images shown are representative of two to four experiments.
	Figure 4. Lmo7 promotes actomyosin bundle formation at the medioapical cortex. GFP-Lmo7 RNA (1 ng) was injected into one blastomere of four- to eight-cell stage embryos. Images show the superficial ectoderm of stage 11 embryos co-stained with phalloidin or NMIIA antibodies. (A-D″) F-actin accumulation at the medioapical cortex in cells expressing GFP-Lmo7. Areas marked by rectangles in A-A″ are enlarged in B-D″. x-y views and x-z views are shown for uninjected cells (B-B″) and cells expressing low (C-C″) and high (D-D″) levels of GFP-Lmo7. (E-F″) NMIIA accumulation at the medioapical cortex in GFP-Lmo7-expressing cells. Areas marked by rectangles are enlarged in F-F″. x-y view and x view are shown. (G) Quantification of medioapical GFP-Lmo7 and F-actin related to images in A-D″. Fluorescence intensities of medioapical GFP-Lmo7 (x-axis) and phalloidin (y-axis) are shown. Each dot represents one cell. GFP-Lmo7 increases the accumulation of F-actin at the medioapical cortex in a dose-dependent manner. Scale bars: 10 µm. Images shown are representative of two to four experiments.
	Figure 5. Effects of Lmo7 on actomyosin contractility require the Rho-ROCK-NMII pathway. (A-D) Pigment granule accumulation at stage 11. Two blastomeres of four- to eight-cell stage embryos were injected with relevant RNA. (A) Control uninjected and (B) Flag-Lmo7-treated (500 pg RNA) embryos. (C) Embryos injected with Flag-Lmo7 (500 pg RNA) and ROK-C (200 pg RNA), and (D) embryos injected with Flag-Lmo7 (500 pg RNA) and Mypt1CA (50 pg RNA). Images are representative of three experiments. (E-F′) The en face view of the ectodermal cells expressing GFP-Lmo7 alone (200 pg RNA) (E,E′) or together with MyptCA (50 pg RNA) (F,F′). Asterisks indicate cells expressing relevant proteins. (G) Quantification of the apical surface area related to images in E-F″. Individual data points are included with the median indicated by a horizontal line. (H-M) Lmo7 modulates RFP-HA-Wtip localization. (H) Experimental design. Embryos were sequentially injected into a ventral blastomere with RFP-HA-Wtip RNA (200 pg) (in red, four- to eight-cell stage) and GFP-Lmo7 RNA (500 pg) (in yellow, 16- to 32-cell stage), causing protein co-expression in 25-50% cells at stage 11 (asterisks in I-I″). (I-I″) RFP-HA-Wtip puncta localization in cells with or without GFP-Lmo7. Areas in I-I″ are enlarged in J-K″. RFP-HA-Wtip forms puncta near apical junctions and the apical cortex in the absence of Lmo7. (J-K″) Effects of Lmo7 on RFP-HA-Wtip puncta formation near apical junctions. RFP-HA-Wtip forms a smooth line between the Flag-Lmo7 double bands (K-K″). (L) Quantification of the Lmo7 effect on RFP-HA-Wtip puncta formation near the apical cortex. Cells with and without apical Wtip puncta were counted in the control (−Lmo7, n=154) and Lmo7-expressing cells (+Lmo7, n=129). (M) Quantification of the Lmo7 effect on RFP-HA-Wtip puncta near apical junctions. Fluorescence intensity of RFP-HA-Wtip near apical junctions was measured. Scale bars: 500 µm in A; 10 µm in E and I; 2 µm in J and K. Statistical significance of the difference was assessed by the Mann–Whitney U-test.
	Figure 6. Identification of Lmo7 domains required for apical constriction. (A) Structure of Lmo7 and the mutants used in this study. Lmo7 has the N-terminal calponin homology (CH) domain, DUF4757, the α-actinin binding region, the PDZ domain, two coiled-coil domains and the C-terminal LIM domain. (B-I) Representative images of stage 11 embryos injected with RNA encoding various Lmo7 constructs (1 ng). Apical constriction was assessed by pigment granule accumulation. Apical constriction induced by Lmo7 constructs lacking the LIM domain (B), and the coiled-coil and PDZ domains (C). Deletion of the α-actinin-binding region (D) and DUF4757 (E) eliminates the activity of pigment granule accumulation, whereas CH domain deletion has no visible effect (F). Lmo7(aa 400-1274) lacking DUF4757 has no pigment granule accumulation activity (G). The region containing the DUF4757 domain and α-actinin-binding region Lmo7(aa 242-709) was the shortest fragment that induced pigment granule accumulation (H). The DUF4757 domain has no effect on its own (I). (K-L′) Effects of GFP-Lmo7(aa 242-709) and GFP-Lmo7(aa 242-400) on apical domain size. GFP-Lmo7 deletion mutants were mosaically expressed by RNA injection (500 pg, asterisks) in four- to eight-cell stage embryos. GFP fluorescence and phalloidin staining are shown in stage 11 ectoderm. (M) Quantification of apical surface domain size related to K-L′. Apical domain surface size of control cells was measured only in cells that shared at least one cell boundary with cells expressing GFP-Lmo7 mutants. Images for scoring were taken from at least five embryos. Data are representative of more than three independent experiments. Individual data points are included with the median indicated by a horizontal line. Scale bars: 500 µm in B-I; 10 µm in K,L. Statistical significance of the difference was assessed by the Mann–Whitney U-test.
	Figure 7. The DUF4757 domain binds to NMII heavy chain. (A) NMIIA and NMIIB co-precipitate with Flag-Lmo7 in HEK293 T cells. Asterisks indicate protein bands corresponding to full-length or deletion mutant forms of Lmo7. Lmo7(aa 242-400) containing DUF4757 is sufficient to co-precipitate endogenous NMIIA and NMIIB. (B) The alignment of DUF4757/NMIIBD sequences. Xenopus laevis Lmo7 (NM_001135230), Mus musculus Lmo7 (XM_006519190), Danio rerio Lmo7 (XM_021478660), Xenopus laevis LIMCH1 (NM_001096206), Mus musculus LIMCH1 (NM_001001980), Danio rerio LIMCH1 (XM_009291008), Ciona intestinalis Lmo7 (XM_002128910) and Drosophila melanogaster Smallish (NM_169014). Conserved positively charged, negatively charged, hydrophobic or hydrophilic amino acids are marked by red, blue, green and purple, respectively. Ser or Thr residues are marked by light blue. Consensus sequence based on amino acid similarity (>70%) is shown at the bottom. The conserved WQ-WK sequence used for AA-AA substitution is indicated.
	Figure 8. Lmo7 recruits NMII to apical junctions through NMIIBD. Embryos at the four- to eight-cell stage were injected with RNAs (0.5-1 ng) encoding full-length or mutant forms of Lmo7. The superficial ectoderm was imaged at stage 11 after staining using anti-Flag, GFP or NMIIA antibodies. Cells expressing Flag-Lmo7 constructs are marked by asterisks. (A-B′) Lmo7(AAAA) does not cause NMIIA enrichment at apical junctions. Areas marked by rectangles in A and A′ are enlarged in B and B′. (C,C′) NMIIA enrichment in embryo expressing Flag-Lmo7, for comparison purposes. (D-E′) Lmo7(aa 242-709) increases NMIIA accumulation. Areas marked by rectangles in D and D′ are enlarged in E and E′. (F,F′) NMIIA enrichment in embryo expressing GFP-Lmo7, for comparison purposes. (G-I) Quantification of NMIIA accumulation at apical junctions in cells expressing GFP-Lmo7 (G), Flag-Lmo7(AAAA) (H) or GFP-Lmo7(aa 242-709) (I). Fluorescence intensity of NMIIA was measured at 3-10 locations within individual cell-cell boundaries. GFP-Lmo7(242-709) recruits NMIIA less effectively than full-length Lmo7. Boxes and whiskers indicate the lower and upper quartiles, and variabilities outside the upper and lower quartiles. Statistical significance of the difference was assessed by the Mann–Whitney U-test. Scale bars: 10 µm.
	Figure 9. Lmo7 recruits NMII to apical junctions through NMIIBD. Embryos at the four- to eight-cell stage were injected with RNAs (0.5-1 ng) encoding full-length or mutant forms of Lmo7. The superficial ectoderm was imaged at stage 11 after staining using anti-Flag, GFP or NMIIA antibodies. Cells expressing Flag-Lmo7 constructs are marked by asterisks. (A-B′) Lmo7(AAAA) does not cause NMIIA enrichment at apical junctions. Areas marked by rectangles in A and A′ are enlarged in B and B′. (C,C′) NMIIA enrichment in embryo expressing Flag-Lmo7, for comparison purposes. (D-E′) Lmo7(aa 242-709) increases NMIIA accumulation. Areas marked by rectangles in D and D′ are enlarged in E and E′. (F,F′) NMIIA enrichment in embryo expressing GFP-Lmo7, for comparison purposes. (G-I) Quantification of NMIIA accumulation at apical junctions in cells expressing GFP-Lmo7 (G), Flag-Lmo7(AAAA) (H) or GFP-Lmo7(aa 242-709) (I). Fluorescence intensity of NMIIA was measured at 3-10 locations within individual cell-cell boundaries. GFP-Lmo7(242-709) recruits NMIIA less effectively than full-length Lmo7. Boxes and whiskers indicate the lower and upper quartiles, and variabilities outside the upper and lower quartiles. Statistical significance of the difference was assessed by the Mann–Whitney U-test. Scale bars: 10 µm.
	Fig. S1. GFP-Lmo7 co-expression rescues increased apical domain expansion in lmo7 morphants (A) Schematic diagram of the experimental design. lmo7 ATG MO (30 ng) was injected into two ventral blastomeres of four-cell embryos (red). At 16-32 cell stage, RNA encoding control GFP (100 pg) or GFP-Lmo7 (100 pg) was injected into one of the ventral blastomeres (yellow). This sequential injection minimizes non- specific binding of morpholinos to RNA in the injection mixture. (B-B”) Representative image of the boundary between Lmo7MO cell clusters with Lmo7MO+GFP-Lmo7 cell clusters. Embryos were co-stained by phalloidin to outline the apical domain of individual cells. (C) Quantification of apical domain surface size. Control uninjected cells (n=96), lmo7-ATGMO+GFP cells (n=94) and lmo7-ATGMO+GFP-Lmo7 cells from more than five different embryos. Statistical significance of the difference between the median values was assessed by Dunn's test using a Bonferonni correction for the p-values. Scale bar: 10 μm in B.
	Fig. S2. Lmo7 promotes a-actinin enrichment in perijunctional actomyosin bundles RNA encoding GFP-a-actinin 4 (200 pg) was injected into 4-8 cell stage embryos with or without RNA encoding HA-Lmo7 (500 pg). (A, B) GFP-a-actinin 4 localizes at apical junctions and forms a single band. An area marked by a rectangle in A is enlarged in B. (C-D”) HA-Lmo7 promotes GFP- a-actinin 4 association with apical junctions. Areas marked by rectangles in C-C’ are enlarged in D-D”. GFP-a-actinin 4 forms thick double bands that largely overlap HA-Lmo7. Scale bars: 10 μm in A and C. 2 μm in D.
	Fig. S3. Expression levels of GFP-Lmo7 constructs in Xenopus embryos GFP-Lmo7 construct RNAs (1 ng) were injected into 4-8 cell stage embryos. Total embryo lysates were collected at stage 11. Expression levels of GFP-tagged Lmo7 constructs were assessed by immunoblotting with anti-GFP antibodies. Long exposure of the sample from GFP-Lmo7-expressing embryos is shown on the left panel.
	Fig. S4. The DUF4757 domain binds NMII heavy chains and is required for Lmo7-mediated apical constriction (A) Flag-tagged DUF4757 (wt), DUF4757 (WQWK->AAAA), or DUF4757 (WQWK->AAAK) were transfected into HEK293T cells. Cell lysates were immunoprecipitated with anti-Flag antibody. Co-immunoprecipitation of endogenous NMIIA and NMIIB was examined by western blot. (B-E) Representative images of apical pigment granule accumulation in embryos expressing Lmo7 (wt), Lmo7(AAAK), and Lmo7(AAAA). Relevant RNA was injected into two blastomeres of 4-8 cell Xenopus embryos. Scale bar: 500 μm in B.
	Fig. S5. The subcellular localization and effects of GFP-Lmo7(aa 242-709) on F-actin RNAs were injected into 4-8 cell embryos. At stage 11, the embryos were fixed and the ectoderm was stained with phalloidin (A-F”, I-I’), or anti-GFP and NMIIA antibodies (G, G’). (A-F”) The subcellular localization of GFP-Lmo7 (A-B”), GFP-Lmo7(aa 242-709), and GFP-Lmo7(aa 242-400) after injection of 200 pg of each RNA. x-y view (A-A’, C-C’, E-E’) and x-z view (B-B”, D-D”, F-F). Note that both Lmo7(aa 242-709)(C-D”) and Lmo7(aa 242-400) show more localization at the apical cortex, compared to full-length Lmo7. (G-H) The effects of GFP-Lmo7(aa 242-400)(1 ng RNA) on NMIIA in stage 11 ectoderm. (G-G’) Ectodermal cells expressing GFP-Lmo7(aa 242-400)(asterisks). (H) Quantification of GFP-Lmo7(aa 242-400) effects on NMIIA at apical junctions. Fluorescent intensity of NMIIA was measured on individual cell-cell boundaries. (I-J) The effects of GFP-Lmo7(aa 242-709)(1 ng RNA) on F-actin in stage 11 ectoderm. (I, I’) Ectodermal cells expressing GFP- Lmo7(aa 242-709)(asterisks). (J) Quantification of F-actin accumulation at apical junctions. Fluorescence intensity of phalloidin was measured at 3-10 locations within individual perijunctional F-actin bundles. Statistical significance of the difference between the median values was assessed by the Mann-Whitney U test. Data are representative of three independent experiments. Scale bar: 10 μm.
	Fig. S6. Lmo7 expression in Xenopus embryos (A) Lmo7l and Lmo7s expression was examined by RT-PCR. Both Lmo7l and Lmo7s are expressed maternally and zygotically throughout early embryonic development. (B-O) Expression of Lmo7l was examined by in situ hybridization. (B, D, F-N) Lmo7l antisense probes. (C, E, O) Lmo7l sense probes. Asterisks in B, C represent the blastopore. A: anterior. P: posterior. D: dorsal. V: ventral. nt: neural tube. pm: paraxial mesoderm. pe: preplacodal ectoderm. ht: heart. st: somites. pa: pharyngeal arches.
	Fig. S7. Lmo7 knockdown delays neural tube closure (A) Schematics of Lmo7 splicing blocking morpholino (Lmo7-spMO) design. Lmo7-spMO is designed to target the splicing donor site of exon 2. Lmo7-spMO sequence show 100 and 84% match to Lmo7l and Lmo7s, respectively. (B) RT- PCR results of Lmo7l and Lmo7s transcripts in Lmo7-spMO injected embryos. Note the appearance of lower bands. DNA sequencing of these bands confirmed the absence of the exon 2 and premature stop codon (shown in A). (C) Neural tube closure delay in Lmo7 knockdown embryos, related to Figure 9L. X-axis and Y-axis represent the widest distance from the midline to the edge of the neural fold in the control uninjected side and the injected side, respectively.
	Fig. S8. Sequence alignment of DUF4757/NMIIBD among mouse Lmo7 splice variants The DUF4757/NMIIBD were compared among three splice variants of Mus musculus Lmo7; NM_001135230, XM_036158702 and NM_001347628. Evolutionally conserved positively charged, negatively charged, hydrophobic and hydrophilic amino acids are marked by red, blue, green and purple as shown in Figure 7B. Conserved Ser/Thr are marked by light blue.

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